KR20230030032A - 펩타이드 백신의 제형 - Google Patents
펩타이드 백신의 제형 Download PDFInfo
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- KR20230030032A KR20230030032A KR1020237005809A KR20237005809A KR20230030032A KR 20230030032 A KR20230030032 A KR 20230030032A KR 1020237005809 A KR1020237005809 A KR 1020237005809A KR 20237005809 A KR20237005809 A KR 20237005809A KR 20230030032 A KR20230030032 A KR 20230030032A
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Abstract
본 발명은 신규한 재구성 조성물, 상기 재구성 조성물을 포함하는 약학 조성물 및 키트에 관한 것이다. 본 발명은 또한 상기 약학 조성물을 사용한 치료 방법 및/또는 의약으로서 사용하기 위한 약학 조성물에 관한 것이다. 건조된 펩타이드를 재구성하는 방법 및 본 발명의 재구성 조성물을 사용하여 약학 조성물을 제조하는 방법이 또한 제공된다.
Description
본 발명은 의학 및 면역학 분야에 속한다. 특히, 본 발명은 백신 접종용 펩타이드를 재구성하기 위한 신규한 조성물에 관한 것이다. 상기 조성물은 특히 오일-기반 애주번트(adjuvant)를 추가로 포함하는 약학 펩타이드-기반 백신의 제조에 적합하다.
임상 결과는 성공적인 치료 백신 접종의 시대가 왔음을 보여주었다. HPV로 인한 전암성 병변의 경우 병변의 회귀가 나타났으며, 장기 생존의 임상적 이점이 확립되었다. 긴 합성 펩타이드를 기반으로 한 백신은 최적의 백신 플랫폼 중 하나이다. 펩타이드 백신 또는 펩타이드-기반 백신은 지속 감염(persistent infection) 및 암의 치료를 위해, 바람직하게는 바이러스성 항원, 암-항원 및/또는 신-항원을 발현하는 세포를 제거하기 위해 면역계를 표적으로 하는 만성 감염 및 암의 치료를 위해 개발된다. 항원-발현 세포를 제거할 수 있는 항원-특이적인 세포 독성 T 세포를 표적으로 하는 효과적인 세포성 면역 반응(CD4+ 및 CD8+ T-세포 반응)을 유도할 수 있는 펩타이드-기반 백신이 당업계에서 알려져 있다. 선택되는 항원에는 돌연변이 서열, 선택된 암 고환 항원 및 바이러스성 항원이 포함된다(Melief et al. 2016 Journal of Clinical Investigation, Vol 125(9) pages 3401-3412 참조).
펩타이드-기반 백신의 과제 중 하나는 물리적으로 그리고 화학적으로 안정한 주사가능한 용액을 제공하는 것이다. 이는 특히 하나 이상의 펩타이드 및 오일-기반 애주번트를 포함하는 펩타이드-기반 백신 에멀젼에 대한 과제이다. 주사가능한 백신 용액은 전형적으로 출발 물질로서 건조되고, 대부분 동결건조된 펩타이드를 사용하여 환자에게 투여하기 약 1 내지 3시간 전에 현장에서 제조된다. 따라서, 건조된 펩타이드를 신속하게 재구성할 수 있으며, 이어서 오일-기반 보조제와 용이하게 혼합되어, 환자에게 투여하기 전에 실온에서 적어도 2 내지 3시간 동안 물리적으로 그리고 화학적으로 안정한 에멀젼을 생성할 수 있는 적합한 재구성 조성물이 필요하다.
도 1: 용해 후 2시간 실온에서 저장한 3가지 상이한 용매 혼합물 중의 DP-6P(SEQ ID NOs: 1-6으로 표시되는 SLPs를 포함함)의 UPLC 크로마토그램. A) 물에 750μL의 0.1M 시트르산, 프로필렌 글리콜 62.5μL, 에탄올 125μL 및 Cremophor EL 62.5μL의 혼합물에 용해된 DP-6P(총 펩타이드 2.40mg); B) 20%v/v DMSO/물에 용해된 DP-6P(2.40mg 총 펩타이드); C) 10mM DTT를 함유한 20%v/v DMSO/물에 용해된 DP-6P(총 펩타이드 2.40mg).
도 2: 두개의 상이한 용매 혼합물 및 용해 후 두 시점(t=0 및 t=2h)에서 DP-6P(SEQ ID NOs: 1-6으로 표시되는 SLPs를 포함함)의 UPLC 크로마토그램. 두 용매 혼합물 모두 프로필렌 글리콜, 에탄올, 물 및 안정제 또는 환원제를 함유한다. A) t=0에서 물 600μL, 프로필렌 글리콜, 267μL, 에탄올 133μL, 아스코르빅산 1mg/mL의 혼합물에 용해된 DP-6P(총 펩타이드 2.40mg), B) t=2h에서 WFI 600μL, 프로필렌 글리콜 267μL, 에탄올 133μL 및 아스코르빅산 1mg/mL의 혼합물에 용해된 DP-6P(총 펩타이드 2.40mg) C) t=0에서 물에 용해된 750μL의 0.1M 시트르산, 프로필렌 글리콜 62.5μL, 에탄올 125μL 및 Cremophor EL 62.5μL의 혼합물에 용해된 DP-6P(총 펩타이드 2.40mg); D) t=2h에서 물에 용해된 750μL의 0.1M 시트르산, 프로필렌 글리콜 62.5μL, 에탄올 125μL 및 Cremophor EL 62.5μL의 혼합물에 용해된 DP-6P(총 펩타이드 2.40mg).
도 3: 2개의 상이한 용매 혼합물 중의 DP-6P(SEQ ID NOs: 1-6으로 표시되는 SLPs를 포함함)의 UPLC 크로마토그램. 모든 용매 혼합물은 mL 당 물에 용해된 750μL 0.1M 시트르산, 62.5μL 프로필렌 글리콜, 125μL 에탄올 및 Tween20 또는 Cremophor EL(62.5μL)을 함유한다. A) t = 0에서 Tween20을 포함하는 용매 혼합물에 용해 된 DP-6P (2.40 mg 총 펩타이드); B) Tween20을 포함하는 용매 혼합물에 용해 된 DP-6P (총 펩타이드 2.40 ㎎)를 t = 2 시간; C) t = 0에서 Cremophor EL을 포함하는 용매 혼합물에 용해 된 DP-6P (2.40 mg 총 펩타이드); D) Cremophor EL을 포함하는 용매 혼합물에 용해 된 DP-6P (2.40 mg 총 펩타이드)를 t = 2 시간에서.
도 4: Montanide ISA 51 VG로 재구성 및 에멀젼화시킨 후 DP-6P(SEQ ID NOs: 1-6으로 표시되는 SLPs를 포함함) 및 DP-7P(SEQ ID NOs: 7-13으로 표시되는 SLPs를 포함함)의 UPLC 크로마토그램이다. 재구성을 위한 용매 혼합물은 mL 당 물에 용해된 750μL 0.1M 시트르산, 62.5μL 프로필렌 글리콜, 125μL 에탄올 및 Cremophor EL(62.5μL)을 함유한다. 분석 전에, 과량의 용매 혼합물을 첨가하고 원심분리에 의해 상분리를 강제로 함으로써 에멀젼으로부터 펩타이드를 추출하였다. A) t=0에서(백신 제조 및 추출 직후) Cremophor EL을 포함하는 1mL 용매 혼합물에 용해된 DP-6P(2.4mg 총 펩타이드); B) t=2h에서(추출 후 백신 생성물 저장 2시간 후) Cremophor EL을 포함하는 1mL 용매 혼합물에 용해된 DP-6P(2.4mg 총 펩타이드); C) t=0에서(백신 제조 및 추출 직후) Cremophor EL을 포함하는 1mL 용매 혼합물에 용해된 DP-7P(2.8mg 총 펩타이드); D) t=2h에서(추출 후 백신 생성물 저장 2시간 후) Cremophor EL을 포함하는 1mL 용매 혼합물에 용해된 DP-7P(2.8mg 총 펩타이드).
도 5: 2개의 상이한 시트르산 농도를 사용한 DP-6P 에멀젼 사이의 입자 크기 분포 비교(오버레이). 물에 용해된 750μL 0.05M 또는 0.1M 시트르산, 62.5μL 프로필렌 글리콜, 125μL 에탄올 및 62.5μL Cremophor EL의 혼합물에 용해되고, 후속적으로 1 mL의 Montanide ISA51 VG로 에멀젼화된 DP-6P(2.40 mg 총 펩타이드).
도 6: DP-6P 에멀젼(SEQ ID NOs: 1-6으로 표시되는 SLPs를 포함함) 사이의 입자 크기 분포 비교(오버레이). DP-6P(2.40mg 총 펩타이드)를 물에 용해된 750μL 0.1M 시트르산, 62.5μL 프로필렌 글리콜, 125μL 에탄올 및 62.5μL Cremophor EL 의 혼합물에 용해하고, 후속적으로 1 mL Montanide ISA51 VG로 에멀젼화시켰다. A) t=0에서 세 가지 독립적인(반복된) 제조물(prep1, prep2 및 prep3)로서 에멀젼화 방법의 견고성을 나타냄. B) t=0(prep1t0h 및 prep1t2h) 및 t=2h(prep2t0h 및 prep2t2h)에서 두 가지 독립적인(반복된) 제조물로서 에멀젼화 방법의 견고함과 실온에서 적어도 2시간 동안 에멀젼의 사용 중 물리적 안정성을 입증함.
도 7: TC- 종양 실험을 위한 타임라인
도 8: (A) Montanide 단독으로 1:1로 에멀젼화된 40%v/v DMSO/WFI(DMSO), (B) Montanide 단독으로 1:1로 에멀젼화된 재구성(Rec.) 조성물(물에 용해된 750μL 0.1M 시트르산, 62.5μL 프로필렌 글리콜 및 125μL 에탄올 및 Cremophor EL 62.5μL)(Rec. 조성물), 또는 (C) Montanide로 1:1로 에멀젼화된 40%v/v DMSO/WFI에 용해된 SEQ ID NO: 6으로 표시되는 SLP 및 CpG ODN1826(DMSO + SLP) 또는 (D) Montanide로 1:1로 에멀젼화된 재구성(Rec.) 조성물(물에 용해된 750μL 0.1M 시트르산, 62.5μL 프로필렌 글리콜 및 125μL 에탄올 및 Cremophor EL 62.5μL)에 용해된 SEQ ID NO: 6으로 표시되는 SLP 및 CpG ODN1826(Rec. 조성물 + SLP)로 백신 접종된 마우스에서 TC-1 종양의 증식물.
도 9: TC-1 종양을 접종하고, 후속적으로 Montanide 단독으로 1:1로 에멀젼화된 40%v/v DMSO/WFI(DMSO)으로 백신 접종된 그룹 1 마우스, TC-1 종양을 접종하고, 후속적으로 Montanide 단독으로 1:1로 에멀젼화된 재구성(Rec.) 조성물(물에 용해된 750μL 0.1M 시트르산, 62.5μL 프로필렌 글리콜 및 125μL 에탄올 및 Cremophor EL 62.5μL)(Rec. 조성물)로 백신 접종된 그룹 2 마우스, TC-1 종양을 접종하고, 후속적으로 Montanide로 1:1로 에멀젼화된 40%v/v DMSO/WFI에 용해된 SEQ ID NO: 6으로 표시되는 SLP 및 CpG ODN1826(DMSO + SLP)으로 백신 접종된 그룹 3 마우스 및 TC-1 종양을 접종하고, 후속적으로 Montanide로 1:1로 에멀젼화된 재구성(Rec.) 조성물(물에 용해된 750μL 0.1M 시트르산, 62.5μL 프로필렌 글리콜 및 125μL 에탄올 및 Cremophor EL 62.5μL)에 용해된 SEQ ID NO: 6으로 표시되는 SLP 및 CpG ODN1826(Rec. 조성물 + SLP)으로 백신 접종된 그룹 4 마우스의 Kaplan-Meier 플롯(생존)(A) 및 유도된 Db-RAYNIVTF(테트라머) 양성 CD8+ T 세포의 퍼센트(B). 별표(asterisk)는 유의한 차이를 나타낸다(unpaired t-test, p=0.022); ns는 유의하지 않은 차이를 나타낸다(p=0.21).
도 10: P53 DP-5P(SEQ ID NO: 191, 193, 194, 201 및 203으로 표시되는 SLPs를 포함함)의 UPLC 크로마토그램. P53 DP-5P를 mL 당 물에 용해된 750μL 0.1 M 시트르산, 62.5μL 프로필렌 글리콜, 125μL 에탄올 및 Cremophor EL(62.5μL)을 함유하는 용매 혼합물로 재구성하였다. 분석하기 전에, 과량의 용매 혼합물을 첨가하고 원심분리에 의해 상분리를 강제하여 펩타이드를 최종 생성물 에멀션으로부터 추출하였다. A) t=0에서(백신 제조 및 추출 직후) Cremophor EL을 포함하는 1mL 용매 혼합물에 용해된 P53 DP-5P(2.0mg 총 펩타이드); B) t=2h에서(추출 후 백신 생성물의 2시간 저장 후) Cremophor EL을 포함하는 1mL 용매 혼합물에 용해된 P53 DP-5P(2.0mg 총 펩타이드).
도 2: 두개의 상이한 용매 혼합물 및 용해 후 두 시점(t=0 및 t=2h)에서 DP-6P(SEQ ID NOs: 1-6으로 표시되는 SLPs를 포함함)의 UPLC 크로마토그램. 두 용매 혼합물 모두 프로필렌 글리콜, 에탄올, 물 및 안정제 또는 환원제를 함유한다. A) t=0에서 물 600μL, 프로필렌 글리콜, 267μL, 에탄올 133μL, 아스코르빅산 1mg/mL의 혼합물에 용해된 DP-6P(총 펩타이드 2.40mg), B) t=2h에서 WFI 600μL, 프로필렌 글리콜 267μL, 에탄올 133μL 및 아스코르빅산 1mg/mL의 혼합물에 용해된 DP-6P(총 펩타이드 2.40mg) C) t=0에서 물에 용해된 750μL의 0.1M 시트르산, 프로필렌 글리콜 62.5μL, 에탄올 125μL 및 Cremophor EL 62.5μL의 혼합물에 용해된 DP-6P(총 펩타이드 2.40mg); D) t=2h에서 물에 용해된 750μL의 0.1M 시트르산, 프로필렌 글리콜 62.5μL, 에탄올 125μL 및 Cremophor EL 62.5μL의 혼합물에 용해된 DP-6P(총 펩타이드 2.40mg).
도 3: 2개의 상이한 용매 혼합물 중의 DP-6P(SEQ ID NOs: 1-6으로 표시되는 SLPs를 포함함)의 UPLC 크로마토그램. 모든 용매 혼합물은 mL 당 물에 용해된 750μL 0.1M 시트르산, 62.5μL 프로필렌 글리콜, 125μL 에탄올 및 Tween20 또는 Cremophor EL(62.5μL)을 함유한다. A) t = 0에서 Tween20을 포함하는 용매 혼합물에 용해 된 DP-6P (2.40 mg 총 펩타이드); B) Tween20을 포함하는 용매 혼합물에 용해 된 DP-6P (총 펩타이드 2.40 ㎎)를 t = 2 시간; C) t = 0에서 Cremophor EL을 포함하는 용매 혼합물에 용해 된 DP-6P (2.40 mg 총 펩타이드); D) Cremophor EL을 포함하는 용매 혼합물에 용해 된 DP-6P (2.40 mg 총 펩타이드)를 t = 2 시간에서.
도 4: Montanide ISA 51 VG로 재구성 및 에멀젼화시킨 후 DP-6P(SEQ ID NOs: 1-6으로 표시되는 SLPs를 포함함) 및 DP-7P(SEQ ID NOs: 7-13으로 표시되는 SLPs를 포함함)의 UPLC 크로마토그램이다. 재구성을 위한 용매 혼합물은 mL 당 물에 용해된 750μL 0.1M 시트르산, 62.5μL 프로필렌 글리콜, 125μL 에탄올 및 Cremophor EL(62.5μL)을 함유한다. 분석 전에, 과량의 용매 혼합물을 첨가하고 원심분리에 의해 상분리를 강제로 함으로써 에멀젼으로부터 펩타이드를 추출하였다. A) t=0에서(백신 제조 및 추출 직후) Cremophor EL을 포함하는 1mL 용매 혼합물에 용해된 DP-6P(2.4mg 총 펩타이드); B) t=2h에서(추출 후 백신 생성물 저장 2시간 후) Cremophor EL을 포함하는 1mL 용매 혼합물에 용해된 DP-6P(2.4mg 총 펩타이드); C) t=0에서(백신 제조 및 추출 직후) Cremophor EL을 포함하는 1mL 용매 혼합물에 용해된 DP-7P(2.8mg 총 펩타이드); D) t=2h에서(추출 후 백신 생성물 저장 2시간 후) Cremophor EL을 포함하는 1mL 용매 혼합물에 용해된 DP-7P(2.8mg 총 펩타이드).
도 5: 2개의 상이한 시트르산 농도를 사용한 DP-6P 에멀젼 사이의 입자 크기 분포 비교(오버레이). 물에 용해된 750μL 0.05M 또는 0.1M 시트르산, 62.5μL 프로필렌 글리콜, 125μL 에탄올 및 62.5μL Cremophor EL의 혼합물에 용해되고, 후속적으로 1 mL의 Montanide ISA51 VG로 에멀젼화된 DP-6P(2.40 mg 총 펩타이드).
도 6: DP-6P 에멀젼(SEQ ID NOs: 1-6으로 표시되는 SLPs를 포함함) 사이의 입자 크기 분포 비교(오버레이). DP-6P(2.40mg 총 펩타이드)를 물에 용해된 750μL 0.1M 시트르산, 62.5μL 프로필렌 글리콜, 125μL 에탄올 및 62.5μL Cremophor EL 의 혼합물에 용해하고, 후속적으로 1 mL Montanide ISA51 VG로 에멀젼화시켰다. A) t=0에서 세 가지 독립적인(반복된) 제조물(prep1, prep2 및 prep3)로서 에멀젼화 방법의 견고성을 나타냄. B) t=0(prep1t0h 및 prep1t2h) 및 t=2h(prep2t0h 및 prep2t2h)에서 두 가지 독립적인(반복된) 제조물로서 에멀젼화 방법의 견고함과 실온에서 적어도 2시간 동안 에멀젼의 사용 중 물리적 안정성을 입증함.
도 7: TC- 종양 실험을 위한 타임라인
도 8: (A) Montanide 단독으로 1:1로 에멀젼화된 40%v/v DMSO/WFI(DMSO), (B) Montanide 단독으로 1:1로 에멀젼화된 재구성(Rec.) 조성물(물에 용해된 750μL 0.1M 시트르산, 62.5μL 프로필렌 글리콜 및 125μL 에탄올 및 Cremophor EL 62.5μL)(Rec. 조성물), 또는 (C) Montanide로 1:1로 에멀젼화된 40%v/v DMSO/WFI에 용해된 SEQ ID NO: 6으로 표시되는 SLP 및 CpG ODN1826(DMSO + SLP) 또는 (D) Montanide로 1:1로 에멀젼화된 재구성(Rec.) 조성물(물에 용해된 750μL 0.1M 시트르산, 62.5μL 프로필렌 글리콜 및 125μL 에탄올 및 Cremophor EL 62.5μL)에 용해된 SEQ ID NO: 6으로 표시되는 SLP 및 CpG ODN1826(Rec. 조성물 + SLP)로 백신 접종된 마우스에서 TC-1 종양의 증식물.
도 9: TC-1 종양을 접종하고, 후속적으로 Montanide 단독으로 1:1로 에멀젼화된 40%v/v DMSO/WFI(DMSO)으로 백신 접종된 그룹 1 마우스, TC-1 종양을 접종하고, 후속적으로 Montanide 단독으로 1:1로 에멀젼화된 재구성(Rec.) 조성물(물에 용해된 750μL 0.1M 시트르산, 62.5μL 프로필렌 글리콜 및 125μL 에탄올 및 Cremophor EL 62.5μL)(Rec. 조성물)로 백신 접종된 그룹 2 마우스, TC-1 종양을 접종하고, 후속적으로 Montanide로 1:1로 에멀젼화된 40%v/v DMSO/WFI에 용해된 SEQ ID NO: 6으로 표시되는 SLP 및 CpG ODN1826(DMSO + SLP)으로 백신 접종된 그룹 3 마우스 및 TC-1 종양을 접종하고, 후속적으로 Montanide로 1:1로 에멀젼화된 재구성(Rec.) 조성물(물에 용해된 750μL 0.1M 시트르산, 62.5μL 프로필렌 글리콜 및 125μL 에탄올 및 Cremophor EL 62.5μL)에 용해된 SEQ ID NO: 6으로 표시되는 SLP 및 CpG ODN1826(Rec. 조성물 + SLP)으로 백신 접종된 그룹 4 마우스의 Kaplan-Meier 플롯(생존)(A) 및 유도된 Db-RAYNIVTF(테트라머) 양성 CD8+ T 세포의 퍼센트(B). 별표(asterisk)는 유의한 차이를 나타낸다(unpaired t-test, p=0.022); ns는 유의하지 않은 차이를 나타낸다(p=0.21).
도 10: P53 DP-5P(SEQ ID NO: 191, 193, 194, 201 및 203으로 표시되는 SLPs를 포함함)의 UPLC 크로마토그램. P53 DP-5P를 mL 당 물에 용해된 750μL 0.1 M 시트르산, 62.5μL 프로필렌 글리콜, 125μL 에탄올 및 Cremophor EL(62.5μL)을 함유하는 용매 혼합물로 재구성하였다. 분석하기 전에, 과량의 용매 혼합물을 첨가하고 원심분리에 의해 상분리를 강제하여 펩타이드를 최종 생성물 에멀션으로부터 추출하였다. A) t=0에서(백신 제조 및 추출 직후) Cremophor EL을 포함하는 1mL 용매 혼합물에 용해된 P53 DP-5P(2.0mg 총 펩타이드); B) t=2h에서(추출 후 백신 생성물의 2시간 저장 후) Cremophor EL을 포함하는 1mL 용매 혼합물에 용해된 P53 DP-5P(2.0mg 총 펩타이드).
재구성 조성물
예방 접종을 위해 펩타이드를 재구성하기 위한 신규한 조성물이 제공된다. 이 재구성 조성물은 유기산을 포함하는 약 60-80% v/v 수용액, 약 5-10% v/v 프로필렌 글리콜(CAS no. 57-55-6), 약 10-20% v/v 저급 알코올 및 약 5-10% v/v 비이온성 친수성 계면활성제를 포함하거나 이로 구성된다.
바람직하게, 유기산은 카복실산과 같은 약 유기산이다. 약 유기산은 본원에서 -2 내지 12의 pKa(로그 산 해리 상수)를 갖는 유기산으로 이해되어야 한다. 바람직하게, 약 유기산은 1 내지 10, 또는 2 내지 5 또는 심지어 3 내지 4의 pKa를 갖는다. 약 유기산은 이에 한정하는 것은 아니나, 옥살산(에탄디오익산), 시트르산(2-히드록시프로판-1,2,3-트리카르복실산), 말산(2-히드록시부탄디오익산), 탄산(히드록시메타노익산), 벤조익산(벤젠카르복실산 또는 페닐메타노익산), 포름산(메타노익산), 라틱산(2-히드록시프로파노익산), 아세트산(에타노익산), 부티르산(부타노익산), 발레르산(펜타노닉산), 카프론산(헥사노익산) 및 프로피온산(프로파노익산)으로 구성되는 그룹으로부터 선택된 어느 카르복실산일 수 있다. 가장 바람직하게, 유기산은 시트르산이다.
유기산은 약 0.008 내지 0.25M, 또는 약 0.01 내지 0.2M, 또는 0.05 내지 0.1M 범위의 농도로 수용액 중에 존재할 수 있다. 상기 수용액의 60-80%, 또는 65%-75% 또는 67%-72%, 또는 약 70%를 포함하는 본 발명의 재구성 조성물은 바람직하게 0.05 내지 0.2M, 0.006 내지 0.16M, 0.008 내지 0.12M, 0.03 내지 0.08M, 또는 바람직하게는 0.04 내지 0.6M 범위의 상기 유기산의 생성 농도(resulting concentration)를 갖는다.
저급 알코올은 본원에서 저급 알킬 또는 저급 치환 알킬기의 포화 탄소 원자에 바인딩된 히드록실 작용기를 갖는 유기 화합물로서 이해되며, 여기서 저급 알킬 또는 저급 치환 알킬기는 최대 6개의 탄소 원자를 가지며, 바람직하게는 구조 CH3-(CH2)n-OH를 가지며, 여기서 n=1, 2, 3, 4 또는 5이다. 바람직하게, 저급 알코올은 메탄올, 에탄올, 프로판올, 부탄올 및 펜탄올로 이루어진 그룹으로부터 선택되고, 가장 바람직하게 저급 알코올은 에탄올이다.
비이온성 친수성 계면 활성제는 바람직하게 9 내지 14, 더욱 바람직하게는 12 내지 14의 친수성-친유성 밸런스(HLB) 값을 갖는다. 이 계면활성제는 이에 한정하는 것은 아니나, 소르비탄의 에톡실레이티드 지방산 모노- (특히 5개의 에톡실기), 디- 또는 트리- (특히 20개의 에톡실기) 에스테르를 포함하며, 여기서 지방산은 바람직하게 올리에이트(예, Tween 81®과 같은 에톡실레이티드 소르비탄 모노올리에이트 및/또는 Tween 85®과 같은 에톡실레이티드 소르비탄 트리올리에이트), 팔미테이트, 스테아레이트(예, Tween 65®와 같은 에톡실레이티드 소르비탄 트리스테아레이트), 이소스테아레이트, 라우레이트 및 이의 조합; 에톡실레이티드 지방 알코올(특히 5-10 에톡실기)(예, Brij 76®, Brij 56®, Brij 96®), 에톡실레이티드 지방산(특히 5-10 에톡실기)(예, Simulsol 2599®, Myrj 45®), 에톡실레이티드 캐스터 오일(특히 25-35 에톡실기)(예, Arlatone 650®, Arlatone G®, Cremophor EL®), 및 이의 조합으로 구성되는 그룹으로부터 선택된다.
본 발명의 조성물의 일 구현으로, 비이온성 친수성 계면활성제는
a. 모노-, 디 또는 트리글리세라이드이며, 바람직하게는 에톡실레이티드 트리글리세라이드이며, 그리고/또는
b. 9 내지 14의 친수성-친유성 밸런스(HLB) 값을 갖는다.
HLB 값은 화학식 HLB=20(1-Is/Ia)을 사용하여 계산되며, 여기서 Is는 비누화 지수 또는 비누화 값을 나타내고, Ia는 상기 계면활성제 또는 상기 계면활성제들의 혼합물의 산 지수 또는 산가를 나타낸다. 이 두 가지 지표인 비누화 및 산가는 유럽 약전(8.8 에디션, 각각 2.5.6 및 2.5.1 절)에 설명된 방법에 따라 결정된다.
바람직한 구현으로, 비이온성 친수성 계면활성제는 에톡실레이티드 캐스터 오일, 보다 특히 폴리옥시 35 하이드로게네이티드 캐스터 오일 또는 폴리옥시에틸렌글리세롤트리리시놀리에이트 35(CAS no. 61791-12-6)(예, Cremophor EL®)이며, 이는 캐스터 오일과 에틸렌 옥사이드를 1:35의 몰비로 반응시킴으로써 얻어지는 폴리옥시에틸레이티드 트리글리세라이드의 혼합물이다.
바람직하게, 본 발명의 재구성 조성물은 물에 약 0.1M 시트르산을 포함하는 약 75% v/v 수용액, 약 6.25% v/v 프로필렌 글리콜(CAS no. 57-55-6), 약 12.5% v/v 에탄올 및 약 6.25% v/v 폴리옥시에틸렌글리세롤트리리시놀리에이트 35(CAS no. 61791-12-6)를 포함하거나 이로 구성된다. 환언하면, 재구성 조성물은 물에 약 0.075M 시트르산, 약 6.25% v/v 프로필렌 글리콜(CAS no. 57-55-6), 약 12.5% v/v 에탄올 및 약 6.25% v/v 폴리옥시에틸렌글리세롤트리시놀리에이트 35(CAS no. 61791-12-6)를 포함하거나 이로 구성된다.
또한, 물에 약 0.1M 시트르산을 포함하는 약 75% v/v 수용액, 약 6.25% v/v 프로필렌 글리콜(CAS no. 57-55-6), 약 12.5% v/v 에탄올, 약 6.25% v/v 폴리옥시에틸렌글리세롤트리리시놀리에이트 35(CAS no. 61791-12-6) 및 20μg/mL CpG ODN1826을 포함하거나 이로 구성되는, 또는 물에 약 0.075M 시트르산, 약 6.25% v/v 프로필렌 글리콜(CAS no. 57-55-6), 약 12.5% v/v 에탄올, 약 6.25% v/v 폴리옥시에틸렌글리세롤트리리시놀리에이트 35(CAS no. 61791-12-6) 및 20μg/mL CpG ODN1826을 포함하거나 이로 구성되는 재구성 조성물이 바람직하다.
재구성 조성물은 약학 조성물 하에 하기에 정의된 바와 같은 저장된 펩타이드, 즉 바람직하게는 15 내지 100개의 아미노산 길이를 갖는 펩타이드를 재구성하기에 특히 적합하다. 상기 정의된 길이의 펩타이드를 재구성할 때 안정한 용액을 형성하는 어려움은 당해 기술 분야에서, 특히 상이한 펩타이드, 즉 상이한 아미노산 서열을 가지며 따라서 상이한 화학적 성질을 가지며 물리적으로 다르게 행동하는 경우에 인식된다. 결과적으로, 하나의 동일한 용액에 이들을 재구성하기가 어렵다. 하나 이상의 이들 펩타이드가 시스테인을 포함하는 경우, 그 상부에 SS-브릿지를 형성하는 경향을 처리해야 한다. 분자내 디설파이드 결합이 면역원성을 얻기 위해 백신 펩타이드에서 요구될 수 있지만, 분자간 디설파이드 브릿지 형성은 불안정한 용액을 초래하므로 바람직하지 않다.
본 발명자는 이제 본 발명의 재구성 조성물이 재구성된 펩타이드의 면역원성을 손상시키지 않으면서 분자간 디설파이드 브릿지의 양이 최소화된 고 안정한 재구성된 펩타이드 조성물을 형성하는데 특히 적합함을 확인하였다. 따라서, 본 발명의 재구성 조성물은 이들 펩타이드의 면역원성을 포함하지 않고, 본원에서 추가로 정의된 바와 같이 재구성될 펩타이드의 분자간 디설파이드 형성을 방지한다.
바람직하게는, 본 발명의 재구성 조성물은 대상자, 즉 포유동물 종 또는 인간에게 비경구 투여하기에 적합한 멸균 및/또는 약학-등급 또는 임상-등급 조성물이다. 바람직하게, 본 발명의 재구성 조성물은 GMP(Good Manufacturing Practice)를 사용하여 제조되고 유럽 의약청(European Medicines Agency) 및 FDA(Food and Drug Administration)에 의해 정의된 GMP 품질을 갖는다. 본 발명의 재구성 조성물은 바이얼에 포장될 수 있다. 본 발명은 또한 본원에서 추가로 정의된 단일 약학적 투여량 단위를 재구성하는데, 또는 이의 배수, 즉 2, 3, 4, 5, 6, 7, 8, 9, 10 또는 그 이상의 약학적 투여량 단위를 재구성하는데 적합한 재구성 조성물의 용량을 포함하는 바이얼을 제공한다. 바람직하게, 상기 바이얼은 재구성 조성물이 1개월, 2개월, 3개월, 6개월 또는 1년 또는 심지어 2년 동안 안정한 온도에서 저장된다. 바람직하게, 상기 온도는 -25℃ 내지 25℃, 또는 -23℃ 내지 -18℃, 또는 0℃ 내지 10℃, 또는 2℃ 내지 8℃, 또는 18℃ 내지 23℃이다.
바람직하게, 바이얼에 존재하는 본 발명의 재구성 조성물의 용량은 최대 50 mL, 바람직하게는 0.1 내지 10 mL, 바람직하게는 1 내지 10 mL, 예를 들면, 0.5, 1, 2, 3, 4, 5 또는 10 mL, 또는 그 사이의 임의의 값이다. 바이얼은 본원에서 임의의 형상을 가질 수 있는 용기로서 이해되어야 한다. 선택적으로, 바이얼은 본원에서 주사기로서 이해되어야 한다.
약학 조성물
본 발명의 재구성 조성물은 특히 의약 또는 약학 조성물의 제조를 위한 펩타이드 재구성에 적합하다. 이러한 약학 조성물은 백신, 바람직하게는 펩타이드 백신일 수 있다. "백신"은 지속 감염 및/또는 이형성(metaplasia) 및/또는 형성 장애(dysplasia) 및/또는 신형성(neoplasia)과 관련된 컨디션과 같은 질병의 예방 및/또는 치료를 위한 면역을 생성하기 위해, 선택적으로 추가의 면역 자극 화합물로 보충된 항원 화합물을 포함하는 조성물로서 이해되어야 한다. "펩타이드-기반 백신(peptide-based vaccine)" 또는 "펩타이드 백신(peptide vaccine)"(이들 용어는 본원에서 상호교환적으로 사용됨)은 펩타이드가 활성 성분, 즉 항원성 화합물을 구성하는 백신으로 이해되어야 한다. 바람직하게, 이러한 펩타이드는 긴 합성 펩타이드이다. 보다 바람직하게, CD4+ 및/또는 CD8+ T 세포 반응을 유도할 수 있는 인간 백혈구 항원(HLA)-에피토프를 포함한다.
따라서, 본 발명의 재구성 조성물로 재구성된 펩타이드를 포함하는 약학 조성물이 제공된다. 바람직하게, 본 발명의 약학 조성물은 백신, 바람직하게는 펩타이드-기반 백신이다. 이러한 펩타이드-기반 백신은 지속 감염, 전암성 컨디션 및 암, 바람직하게는 바이러스 항원, 암 고환 항원과 같은 종양-관련 항원 및/또는 발암성 또는 비-발암성 바이러스성 항원과 같은 종양-특이 항원 및/또는 DNA 돌연변이로 인한 신-항원을 발현하는 감염된 전암성 및/또는 암성 세포를 제거하기 위한 세포성 면역계를 활성화시켜 만성 감염, 전암성 컨디션 및 암의 치료에 사용될 수 있다.
약학 조성물은 바람직하게 대상자, 바람직하게는 인간 또는 동물 대상자에 투여하기에 적합하고, 이에 따라 적합하도록 제형화된다. 바람직하게, 투여는 비경 구, 예를 들어, 피하, 근육 내, 피내 및/또는 종양 내 투여, 즉 주사에 의해 투여될 수 있다.
본 발명자들은 재구성된 펩타이드를 포함하는 재구성 조성물이 특히 오일-기반 애주번트와 혼합하여 화학적으로 및 물리적으로 안정한 펩타이드-백신 용액을 형성하는데 적합함을 발견했다.
"화학적으로 안정한(chemically stable)"은 펩타이드 용액 및/또는 펩타이드-백신 조성물과 관련하여 본원에서 언급되며, 예를 들어, 분자내 또는 분자간 디설파이드 브릿지 때문에 수용불가능한 정도로 화학적으로 저하되거나 분해되지 않는 펩타이드를 포함하는 용액 또는 조성물로서 본원에서 이해되어야 하는 것으로, 즉, 용액 및/또는 조성물 내의 비-저하, 비-분해된 그리고/또는 미반응된 펩타이드의 양이, 실온에서 적어도 약 0.5, 1, 1.5, 2 또는 적어도 3시간 동안 용액 또는 조성물을 저장한 후에, 이의 본래 것과 비교하여 적어도 90중량%, 91중량%, 92중량%, 93중량%, 94중량%, 95중량%, 96중량%, 97중량%, 98중량%, 99중량% 또는 심지어 100중량%이다. 화학적 안정성은, 예를 들어, 본원에서 예시된 UPLC/MS를 사용하여 당업계에 공지된 임의의 적합한 기술을 사용하여 평가할 수 있다. UPLC/MS를 사용할 경우, 용액/조성물은 실온에서 적어도 약 0.5, 1, 1.5, 2 또는 적어도 3시간의 저장 후에 나타나는 새로운 피크의 총 % 면적이, 이의 본래 것과 비교하여 최대 20%, 15%, 10%, 9%, 8%, 7%, 6%, 5%, 4%, 3%, 2%, 1%, 또는 0%이면 화학적으로 안정한 것으로 정의되며, 여기서 새로운 피크는 동일한 조건 하에서 측정시 본래 것("본래 것(original)"은 제조 직후 새로 제조된 용액으로 이해됨)의 UPLC 크로마토그램 상으로 확인되지 않은 저장된 용액의 UPLC 크로마토그램 상의 피크인 것으로 이해된다. 바람직하게, 실온에서 3시간 저장 후에 나타나는 새로운 피크의 총 %면적은 동일한 조건 하에서 측정시 이의 본래 것과 비교하여 최대 10%이다.
"물리적으로 안정한(physically stable)"은 본원에서 펩타이드 용액 및/또는 펩타이드-백신 조성물과 관련하여 언급되며, 침전 또는 재분산되지 않는 펩타이드를 포함하는 용액 또는 조성물로 이해되어야 한다. 물리적 안정성은 당업계에 공지 된 임의의 적합한 기술, 예를 들어 육안 검사 또는 본원에 예시된 Malvern Mastersizer를 사용하는 입자 분포에 의해 평가될 수 있으며, 여기서 평균 입자 크기는 D(0.5)로 표시된다. 본원에 예시된 바와 같이 물리적 안정성을 평가하기 위해 Malvern Mastersizer를 사용할 경우, 용액/조성물은 실온에서 적어도 약 0.5, 1, 1.5, 2 또는 적어도 3시간의 저장 후 평균 D(0.5)가 이의 본래 것(즉, 제조 직후에 새로 제조된 용액)과 비교하여 최대 50%, 40%, 30%, 20%, 10% 또는 5% 증가한 경우에 물리적으로 안정한 것으로 정의된다. 바람직하게, 용액/조성물은 실온에서 3시간 저장 후 평균 D(0.5)가 이의 본래 것과 비교하여 최대 50%, 40%, 30%, 20%, 10% 또는 5%, 바람직하게는 최대 20%로 증가한 경우에 물리적으로 안정한 것으로 정의된다.
바람직하게, 본 발명의 약학 조성물은 애주번트를 추가로 포함한다. "애주번트(adjuvant)"라는 용어는 면역-증강 효과를 가지며, 본원에서 대상자에게 투여시 항원 제제에 대한 면역 반응을 강화, 유도, 초래 및/또는 조절하기 위해 첨가되거나 또는 항원 제제와 함께 공동-제형화되는 물질을 지칭하는데 사용된다. 오일-기반 애주번트는 에멀젼(예, 워터-인-오일 또는 오일-인-워터 에멀젼)을 형성하는데 사용될 수 있으며, 당업계에서는 면역 반응을 향상시키고 지시하는 것으로 인식된다. 치료 백신에서 이러한 애주번트의 존재는 매우 유익하다. 따라서, 본 발명은 또한 본 발명의 재구성 조성물, 재구성된 펩타이드 및 오일-기반 애주번트를 포함하거나 또는 이들로 구성된 약학 조성물 또는 약제를 제공하며, 보다 특히, 본 발명은 본 발명의 재구성 조성물의 약 40-60% v/v 및 오일-기반 애주번트의 약 40-60% v/v에 약 0.5-10 mg/mL 펩타이드를 포함하는 약학 조성물을 제공한다.
오일-기반 애주번트는 당업계에 공지된 임의의 미네랄 또는 비-미네랄 오일-기반 애주번트일 수 있다. 바람직하게, 오일-기반 애주번트는 미네랄 오일-기반 애주번트이다. 오일-기반 애주번트의 비제한적 예는 (식물성 오일/어유 등에 기반한) 바이오-기반 오일 애주번트, 스쿠알렌-기반 애주번트(예, MF59), 신텍스 애주번트 제형(Syntex Adjuvant Formulation)(SAF; Lidgate, Deborah M, Preparation of the Syntex Adjuvant Formulation (SAF, SAF-m, and SAF-1), In: Vaccine Adjuvants, Volume 42 of the series Methods in Molecular Medicine?? p229-237, ISSN1543-1894), 프로인드 컴플리트 애주번트(Freund's Complete Adjuvant)(FCA), 프로인드 인컴플리트 애주번트(Freund's Incomplete Adjuvant)(FIA), 땅콩 오일에 기반한 애주번트(예, Adjuvant 65), Lipovant (Byars, N.E., Allison, A.C., 1990. Immunologic adjuvants: general properties, advantages, and limitations. In: Zola, H. (Ed.), Laboratory Methods in Immunology. p39-51), ASO4 (A. Tagliabue, R. Rappuoli Vaccine adjuvants: the dream becomes real Hum. Vaccine, 4 (5), 2008, p347-349), 정제된 스쿠알렌 및 고 정제된 만나이드 모노-올리에이트로 에멀젼화된 스쿠알렌에 기반한 몬타나이드 애주번트(Montanide adjuvants)(예, Montanide ISA 25 VG, 28 VG, 35 VG, 50 V, 50 V2, 51 VG, 61 VG, 70 VG, 70 M VG, 71 VG, 720 VG, 760 VG, 763 A VG, 775 VG, 780 VG, 201 VG, 206 VG, 207 VG)이다. 바람직하게 오일-기반 애주번트는 미네랄 오일-기반 애주번트이다. 보다 바람직하게, 오일-기반 애주번트는 Drakeol VR 및 만나이드 모노올리에이트의 혼합물인 Montanide ISA 51VG(Seppic)이다.
바람직하게, 약학 조성물은 약학적 투여 단위를 구성하는 펩타이드의 양을 포함하거나 또는 이로 구성된다. 본원에서 약학적 투여 단위는 주어진 시점에 대상자에게 적용되는 활성 성분의 양(즉, 펩타이드-기반 백신에서 펩타이드의 총량)으로 정의된다. 약학적 투여 단위는 단일 체적, 즉 단일 샷(single shot)으로 대상자에게 적용될 수 있거나, 또는 예를 들어, 우측 및 좌측 팔다리와 같이 신체의 상이한 위치에 바람직하게 적용되는 2, 3, 4, 5개 이상의 개별 용량 또는 샷으로 적용될 수 있다. 개별 용량으로 단일 약학적 투여 단위를 적용하는 이유는 부작용 회피, 항원 경쟁 회피 및/또는 조성 분석 문제와 같이 여러 가지가 있을 수 있다. 본원에서, 약학적 투여의 개별 용량은 조성이 다를 수 있으며, 즉 상이한 종류 또는 조성의 활성 성분 및/또는 애주번트를 포함할 수 있는 것으로 이해되어야 한다. 전체 약학적 투여 단위 내의 모든 활성 성분(항원성 펩타이드)에 대해, 단일 재구성 조성물이 사용되는데, 이는 본 발명의 이점 중 하나가 본 발명의 재구성 조성물이 재구성, 및 상이한 펩타이드 혼합물의 오일-기반 애주번트를 사용하는 후속적인 에멀젼화에 적합하기 때문이다. 단일 재구성 조성물, 및 바람직하게는 단일 오일-기반 애주번트는 재구성 및 에멀젼화시 사람으로 인한 실패의 가능성을 최소화한다.
총 약학 투여량, 또는 실질적으로 동일한 시점에 적용되는 다중 주사의 경우 그 일부를 포함하는 단일 주사 용량 또는 샷(즉, 특정 시점에서 한 위치에 적용된 용량)은 100 μL 내지 2 mL일 수 있거나 또는 100 μL 내지 1 mL일 수 있다. 단일 주사 용량은 100 μL, 200 μL, 300 μL, 400 μL, 500 μL, 600 μL, 700 μL, 800 μL, 900 μL, 1 mL, 1.1 mL, 1.2 mL, 1.3 mL, 1.4 mL, 1.5 mL, 1.6 mL, 1.7 mL, 1.8 mL, 1.9 mL, 2 mL, 3 mL 또는 그 사이의 임의의 값일 수 있다.
약학적 투여 단위는 유효량 또는 유효량의 일부일 수 있다. "유효량(effective amount)"은 치료되지 않은 환자에 비해 질병(예를 들어, 만성 감염, 전암성 컨디션 및/또는 암)의 증상을 예방 및/또는 감소시키는데 필요한 활성 성분의 양 또는 용량으로서 본원에서 이해되어야 한다. 질병 또는 컨디션의 예방적 및/또는 치료적 처리를 위해 본 발명을 실시하는데 사용되는 활성 화합물(들)의 유효량은 투여 방식, 대상자의 나이, 체중 및 일반적인 건강 상태에 따라 달라진다. 궁극적으로, 주치의 또는 수의사는 적절한 양 및 투여 요법을 결정할 것이다. 이러한 양을 "유효(effective)"량이라고 한다. 이 유효량은 또한 치료될 대상자에서 효과적인 세포성 T 세포 반응, 또는 보다 바람직하게는 효과적인 전신 세포성 T 세포 반응을 유도할 수 있는 양일 수 있다.
바람직하게, 특정 시점에 단일 또는 다중 주사로, 주어진 시점에 대상자에게 적용되는 펩타이드의 약학적 투여 단위, 또는 총량은 약 0.1 μg, 0.5 μg, 1 μg, 5 μg, 10 μg, 15 μg, 20 μg, 30 μg, 40 μg, 50 μg, 60 μg, 70 μg, 80 μg, 90 μg, 100 μg, 150 μg, 200 μg, 250 μg, 300 μg, 350 μg, 400 μg, 450 μg, 500 μg, 650 μg, 700 μg, 750 μg, 800 μg, 850 μg, 900 μg, 1 mg, 1,5 mg, 2 mg, 2.5 mg, 3 mg, 3.5 mg, 4 mg, 4.5 mg, 5 mg, 5.5 mg, 6 mg, 6.5 mg, 7 mg, 7.5 mg, 8 mg, 8.5 mg , 9 mg , 9.5 mg, 10 mg, 15 mg 또는 약 20 mg 또는 그 사이의 임의의 값과 같이 0.1 ㎍ 내지 20 mg 범위의 펩타이드의 양을 포함한다. 약학적 투여 단위의 바람직한 범위는 0.1 ㎍ 내지 20 mg, 1 ㎍ 내지 10 mg, 10 ㎍ 내지 5 mg, 0.5 mg 내지 2 mg, 0.5 mg 내지 10 mg 또는 1 mg 내지 5 mg 또는 2 내지 4 mg이다.
바람직하게, 약학 조성물은 40-60% v/v의 상기 정의된 재구성 조성물 및 40-60% v/v의 오일-기반 애주번트에 약 1-2 mg/ml 펩타이드를 포함하거나 이로 구성된다. 약학 조성물은 약 40%, 41%, 42%, 43%, 44%, 45%, 46%, 47%, 48%, 49%, 50%, 51%, 52%, 53%, 54%, 56%, 57%, 58%, 59% 또는 60% v/v의 오일-기반 애주번트를 포함하거나 이로 구성될 수 있다. 바람직하게, 약학 조성물은 약 50% v/v의 상기 정의된 재구성 조성물 및 약 50% v/v의 오일-기반 애주번트, 바람직하게 Montanide ISA 51 VG (Seppic)에 약 1-2 mg/ml 펩타이드를 포함하거나 이로 구성된다. 즉, 바람직하게, 약학 조성물은 물에, 약 1-2 mg/ml 펩타이드, 0.038M 시트르산, 약 3.13% v/v 프로필렌 글리콜(CAS no. 57-55-6), 약 6.25% v/v 에탄올, 약 3.13% v/v 폴리옥시에틸렌글리세롤트리리시놀리에이트 35(CAS no. 61791-12-6) 및 약 50%의 오일-기반 애주번트, 바람직하게는 Montanide ISA 51 VG(Seppic)을 포함하거나 이로 구성된다.
본 발명의 약학 조성물은 하나 이상의 추가의 면역 반응 자극 화합물 또는 애주번트를 포함할 수 있다. 유리하게, 본 발명에 따른 약제는 추가로 하나 이상의 합성 애주번트를 포함할 수 있다. 이러한 추가의 면역 반응 자극 화합물 또는 애주번트는 (i) 펩타이드의 재구성 및 상기 정의된 바와 같은 오일-기반 애주번트와의 선택적인 에먼젼화 후에 본 발명에 따른 약학 조성물에 혼합되거나, (ii) 상기 정의된 본 발명의 재구성 조성물의 일부이거나, (iii) 재구성될 펩타이드에 물리적으로 결합되거나 또는 (iv) 치료될 대상자, 포유동물 또는 인간에게 개별적으로 투여될 수 있다. 면역 반응 자극 화합물이 본 발명에 따른 약제와 혼합될 경우, 이는 애주번트로서 서술되며; 개별적으로 투여될 경우, 이는 본원에서 상호교환적으로 사용되는 면역-조절제(immuno-modulatory agent) 또는 면역-모듈레이터(immuno-modulator)로서 서술되는 것으로 이해되어야 한다. 특히 바람직한 것은 Toll-유사 리셉터를 통해 그리고/또는 RIG-1(레티노익산-유도성 유전자 -1) 단백질을 통해 그리고/또는 엔도텔린 리셉터를 통해 작용하는 것으로 알려된 애주번트이다. 선천적인 면역계의 활성화가 가능한 면역 조절 화합물은 TLRs 1-10을 포함하는 Toll-유사 리셉터(TLRs)를 통해 특히 잘 활성화될 수 있다. TLR 리셉터 및 이의 변형 및 유도체를 활성화할 수 있는 화합물은 당업계에 잘 공지되어 있다. TLR1은 박테리아 리포단백질 및 이의 아세틸레이티드 형태에 의해 활성화될 수 있고, TLR2는 그람 양성 박테리아 글리코리피드, LPS, LPA, LTA, 핌브리아(fimbriae), 외막 단백질, 박테리아 또는 숙주로부터의 열 충격 단백질, 및 마이코박테리아 리포아라비노만난에 의해 활성화될 수 있다. TLR3은 특히 바이러스 기원의 dsRNA 또는 화학적 화합물 폴리(I:C)에 의해 활성화될 수 있다. TLR4는 그람 음성 LPS, LTA, 숙주 또는 박테리아 기원의 열 충격 단백질, 바이러스 코트 또는 엔벨로프 단백질, 탁솔 또는 이의 유도체, 올리고사카라이드 및 피브로넥틴을 함유하는 히알루로난에 의해 활성화될 수 있다. TLR5는 박테리아 플라겔라 또는 플라겔린으로 활성화될 수 있. TLR6은 마이코박테리아 리포단백질 및 그룹 B 스트렙토코커스 열 불안정 용해 인자(GBS-F) 또는 스타필로코커스 모듈린에 의해 활성화될 수 있다. TLR7은 이미퀴모드, 레시퀴모드 및 유도체 이미퀴모드 또는 레시퀴모드(예, 3M-052)와 같은 이미다조퀴놀린에 의해 활성화될 수 있다. TLR9는 메틸화되지 않은 CpG DNA 또는 크로마틴-IgG 복합체에 의해 활성화될 수 있다. 특히, TLR3, TLR7 및 TLR9는 바이러스 감염에 대한 선천적인 면역 반응을 매개하는데 중요한 역할을 하며, 이들 리셉터들을 활성화시킬 수 있는 화합물은 본 발명에 따른 조성물 또는 약제에서 특히 바람직하다. 특히 바람직한 애주번트는 이에 한정하는 것은 아니나, dsRNA, 폴리(I:C), 폴리 I:CLC, TLR3 및 TLR9 리셉터를 유발하는 메틸화되지 않은 CpG DNA, IC31, TLR 9 아고니스트, IMSAVAC, TLR 4 아고니스트, Montanide ISA-51, Montanide ISA 720(Seppic(France)에 의해 제조되는 애주번트)을 포함하는 합성적으로 생성된 화합물들을 포함한다. RIG-I 단백질은 TLR3과 마찬가지로 ds-RNA에 의해 활성화되는 것으로 알려져 있다(Kato et al, (2005) Immunity, 1: 19-28). 특히 바람직한 TLR 리간드는 pam3cys 및/또는 이의 유도체, 바람직하게는 pam3cys 리포펩타이드 또는 이의 변이체 또는 유도체이고, 바람직하게는 WO2013051936A1에 기재된 것들, 더욱 바람직하게는 U-Pam12 또는 U-Pam14 또는 AMPLIVANT®이다. 추가로 바람직한 애주번트는 시클릭 디뉴클레오타이드(CDNs), 무라밀 디펩타이드(MDP) 및 폴리-ICLC이다. 바람직한 구현으로, 본 발명의 애주번트는 WO2013051936A1에 기재된 pam3cys 리포펩타이드 유도체, 폴리-ICLC, 이미퀴모드, 레시퀴모드 또는 이의 유도체와 같은 이미다조퀴놀린, 비자연발생 서열을 갖는 CpG 올리고데옥시뉴클레오타이드(CpG-ODNs), 및 비자연발생 아미노산을 포함하는 무라밀 디펩타이드(MDP) 또는 테타너스 톡소이드 펩타이드와 같은 펩타이드-기반 애주번트와 같은 비자연발생 애주번트이다. 더욱 바람직한 애주번트들은 1018 ISS, 알루미늄염, Amplivax, AS 15, BCG, CP-870,893, CpG7909, CyaA, dSLIM, GM-CSF, IC30, IC31, ImuFact EV1P321, IS Patch, ISS, ISCOMATRIX, Juvlmmune, LipoVac, MF59, 모노포스포릴 리피드 A, Montanide IMS 1312, Montanide ISA 206, Montanide ISA 50V, OK-432, OM-174, OM-197-MP-EC, ONTAK, PepTel.RTM, 벡터 시스템, PLGA 마이크로파티클, SRL172, 바이로좀 및 다른 바이러스-유사 파티클, Pam3Cys-GDPKHPKSF, YF-17D, VEGF 트랩, R848, 베타-글루칸, 아퀼라 QS21 스티물론(Aquila's QS21 stimulon), 바디메잔(vadimezan), AsA404(DMXAA), STING(IFN 유전자의 자극제) 아고니스트(예, c-di-GMP VacciGradeTM), PCI, NKT(자연살상 T 세포) 아고니스트(예, 알파-갈락토실세라마이드 또는 알파-GalCer, RNAdjuvant®(Curevac), 레티노익산 유도성 단백질 I 리간드(e.g. 3pRNA 또는 5'-트리포스페이트 RNA)로 구성되는 그룹으로부터 선택된다.
상기 언급한 바와 같이, 애주번트는 재구성될 펩타이드(들)에 물리적으로 결합될 수 있다. 본원에서 하기에 정의된 바와 같은 항원 펩타이드에 대한 애주번트 및 공동자극 화합물 또는 작용기의 물리적 결합은 항원을 내재화, 대사 및 디스플레이하는 항원-제시 세포, 특히 수지상 세포에 대한 개선된 표적화에 의해, 그리고 다양한 공동자극 분자의 발현을 상향조절하도록 이러한 세포들을 동시에 자극하여, 이에 따라 효율적인 T 세포 반응을 유도하고 증진시키는 세포들이 됨으로써 증진된 면역 반응을 제공한다. 또 다른 바람직한 면역 변형 화합물은 BQ-788(Buckanovich RJ et al., (2008) Nature Medicine 14: 28; Ishikawa K, (1994) PNAS 91: 4892), 및/또는 이의 유도체와 같은 엔도텔린 리셉터의 인히비터이다. BQ-788은 N-시스-2,6-디메틸피페리디노카르보닐-L-감마-메틸루실-D-1-메톡시카르보닐트립토파닐-D-노르루신이다. 또 다른 바람직한 면역 반응 자극 화합물 또는 애주번트는 인터페론 알파(IFNα), 보다 바람직하게는 페길레이티드 인터페론 알파이다. 또한, WO99/61065 및 WO03/084999에 개시된 항원 제시 세포 (공동)자극 분자를 본 발명의 펩타이드 및 조성물과 함께 사용하는 것이 바람직하다. 특히, 4-1BB 및/또는 CD40 리간드, 아고니스틱 항체, OX40 리간드, CD27 리간드 또는 이의 기능적 단편 및 이의 유도체뿐만 아니라 유사한 아고니스틱 활성을 갖는 합성 화합물의 사용은 바람직하게, 대상자에서 최적의 면역 반응의 장착을 더욱 자극하기 위해서, 개별적으로 또는 본 발명의 펩타이드와 함께 치료될 대상자에게 투여된다.
본 발명의 재구성 조성물에서 재구성되거나 및/또는 본 발명의 약학 조성물 내에 포함되는 펩타이드는, 바람직하게 약 15 내지 약 100 개의 아미노산 길이를 갖는다. 바람직하게, 재구성되는 펩타이드는 길이가 15-100 개의 아미노산, 또는 15-95 개의 아미노산, 또는 15-90 개의 아미노산, 또는 15-85 개의 아미노산, 또는 15-70 개의 아미노산, 또는 15-65 개의 아미노산, 또는 15-60 개의 아미노산, 또는 15-55 개의 아미노산, 또는 15-50 개의 아미노산, 또는 15-45 개의 아미노산, 또는 15-40 개의 아미노산, 또는 17-39 개의 아미노산, 또는 19-43 개의 아미노산, 또는 22-40 개의 아미노산, 또는 22-45 개의 아미노산, 또는 28-40 개의 아미노산, 또는 30-39 개의 아미노산이다. 바람직하게, 재구성되는 펩타이드는 최대 100, 99, 98, 97, 96, 95, 94, 93, 92, 91, 90, 89, 88, 87, 86, 85, 84, 83, 82, 81, 80, 79, 78, 77, 76, 75, 74, 73, 72, 71, 70, 69, 68, 67, 66, 65, 64, 63, 62, 61, 60, 59, 58, 57, 56, 55, 54, 53, 52, 51, 50, 49, 48, 47, 46, 45, 44, 43, 42, 41, 40, 39, 38, 37, 36, 35, 34, 33, 32, 31, 또는 30 개의 아미노산이다. 바람직하게, 재구성되는 펩타이드는 적어도 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44 또는 45 개의 아미노산이다. 바람직하게, 재구성되는 펩타이드는 적어도 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44 또는 45 개의 아미노산 및 100, 99, 98, 97, 96, 95, 94, 93, 92, 91, 90, 89, 88, 87, 86, 85, 84, 83, 82, 81, 80, 79, 78, 77, 76, 75, 74, 73, 72, 71, 70, 69, 68, 67, 66, 65, 64, 63, 62, 61, 60, 59, 58, 57, 56, 55, 54, 53, 52, 51, 50, 49, 48, 47, 46, 45, 44, 43, 42, 41, 40, 39, 38, 37, 36, 35, 34, 33, 32, 31, 또는 30 개 이하의 아미노산, 또는 이들의 하한 및 상한의 임의의 조합이다.
본 발명의 재구성 조성물에서 재구성되거나 및/또는 본 발명의 약학 조성물 내에 포함되는 펩타이드는 단백질 항원으로부터 유도된 펩타이드일 수 있다. "단백질 항원(protein antigen)"은 본원에서 숙주 동물 또는 인간에서 면역 반응을 유도할 수 있는 항원 영역을 포함하는 단백질 또는 폴리펩타이드로 이해되어야 한다. 감염된, 전암성 세포 및/또는 암성 세포에 의해 특이적으로 발현되는 단백질 항원은 치료 백신의 적합한 표적이다. 이러한 단백질 항원은 바이러스성 또는 비-바이러스성 항원일 수 있다. 예방 백신 및 치료 백신의 표적이 되는 바이러스성 항원의 예는 엡스타인 바 바이러스 유도 림프종(EBV), 인간 T 백혈병 바이러스 I, B형 간염 바이러스(HBV), 인유두종 바이러스(HPV), 카포시 육종 포진 바이러스(KSHV), C형 간염 바이러스(HVC), KSV 및 Merkel 세포 암종 바이러스로부터 유래된 항원들이다. 바이러스 단백질 항원의 비제한적인 예는 EBV로부터의 단백질 항원, 예, LMP1 또는 후기 막 단백질 1(예, UniprotKB P03230) 및 LMP2 또는 후기 막 단백질 2(예, UniprotKB P13285); 인간 T 백혈병 바이러스 I으로부터의 단백질 항원, 예. 택스(Tax) 단백질(예, UniprotKB P14079; P0C213; P03409); HBV로부터의 단백질 항원, 예, 유전자형 A, B, C 또는 D, 예, 단백질 HBsAg(예, UniprotKB Q773S4), X-단백질(예, UniprotKB Q8V1H6) 라지 엔벨로프 단백질(예, UniprotKB P03138) 및 캡시드 단백질(예, UniprotKB P03147); HCV로부터의 단백질 항원, 예, 게놈 폴리프로틴(예, UniprotKB P26663; Q99IB8; A3EZI9) 및 HCV 단백질(예, UniprotKB Q99398); HPV로부터의 단백질 항원, 예, 발암성 유전자형 6, 11, 16 또는 18, 예, E6 종양단백질(예, UniprotKB P03126; P06463) 및 E7 종양단백질(예, UniprotKB P03129; P06788) KSHV로부터의 단백질 항원, 예, 단백질 ORF36(예, UniprotKB F5HGH5), 코어(Core) 유전자 UL42 계열 단백질(예, UniprotKB Q77ZG5), 비리온(Virion) 에그레스 단백질 UL31 호모로그(예, UniprotKB F5H982), 트리플렉스(Triplex) 캡시드 단백질 VP19C 호모로그(예, UniprotKB F5H8Y5), 바이러스 대식세포 염증 단백질 2(예, UniprotKB Q98157), mRNA 익스포트 팩터 ICP27 호모로그(예, UniprotKB Q2HR75), ORF52(예, UniprotKB F5HBL8), 바이러스 IRF4-유사 단백질(예, UniprotKB Q2HR73), Bcl-2(예, UniprotKB Q76RI8), 라지 테그먼트(tegument) 단백질 덴딜라아제(deneddylase)(예, UniprotKB Q2HR64), V-시클린(예, . UniprotKB O40946), VIRF-1(예, UniprotKB F5HF68) 및 E3 유비퀴틴-단백질 리가아제 MIR1(예, UniprotKB P90495) 및 항원 단백질 Merkel 세포 암종 바이러스, 예, 라지 T 단백질(예, UniprotKB E2IPT4; K4P159), 예, 스몰 T 단백질(예, UniprotKB B6DVX0; B6DVX6)이다.
예방 백신 및 치료 백신에 적합한 표적이 되는 비-바이러스성 항원은 종양 특이 항원 및/또는 종양 관련 항원일 수 있다. 종양 특이 항원은 다른 세포가 아닌 종양 세포에 의해 배타적으로 발현되는 항원이며, 종종 KrasG12D 및 돌연변이 P53과 같은 돌연변이된 단백질이거나, 또는 DNA 돌연변이 및 DNA 수복 메커니즘 오작동에 의해 발생하는 네오-항원이다. 종양 관련 항원은 종양 및 정상 세포 모두에 존재하는 내인성 항원이지만, HER-2/neu 리셉터와 같은 이들의 발현 또는 세포 국소화에 조절 장애가 있다. 치료 백신의 표적이 될 수 있는 비-바이러스성 항원의 비제한적인 예는 Her-2/neu (또는 ErbB-2, 인간 표피 성장 인자 리셉터 2(예, UniprotKB P04626); WT-1 또는 Wilms 종양 단백질(예, UniprotKB P19544); NY-ESO-1 또는 암/고환 항원 1(예, UniprotKB P78358); MAGE-A3 또는 멜라노마-관련 항원-A3(예, UniprotKB P43357); BAGE 또는 B 멜라노마 항원(예, UniProtKB Q13072); CEA 또는 암배아성 항원(예, UniProtKB Q13984); AFP 또는 α-페토단백질(예, UniProtKB P02771); XAGE-1B 또는 X 항원 계열 멤버 1(예, UniProtKB Q9HD64); 서비빈(survivin) 또는 BIRC5, 배큘로바이러스 IAP 반복-함유 단백질 5(예, UniprotKB O15392); P53(예, UniprotKB P04637); h-TERT 또는 텔로머라아제 리버스 트랜스크립타아제(예, UniprotKB O14746); 메소텔린(예, UniProtKB H3BR90); PRAME 또는 ㅁ종양에서 우선적으로 발현되는 멜라노마 항원(예, UniprotKB P78395); MUC-1 또는 뮤신-1(예, UniprotKB P15941); Mart-1/Melan-A 또는 T-세포 1에 의해 인식되는 멜라노마 항원(예, UniprotKB Q16655); GP-100 또는 멜라노사이트 단백질 PMEL(예, UniprotKB P40967); 티로시나아제(예, UniprotKB U3M8N0); 티로시나아제-관련 단백질-1(예, UniprotKB P17643); 티로시나아제-관련 단백질-2(예, UniprotKB O75767); PAP 또는 PAPOLA, 폴리(A) 폴리머라아제 알파(예, UniprotKB P51003); PSA 또는 ㅈ전립선-특이 항원(예, UniprotKB P07288); PSMA 또는 전립선-특이 멤브레인 항원, 또는 글루타메이트 카르복시펩티다아제 2(예, UniprotKB Q04609)이다.
펩타이드-백신에 대해 바람직한 종양 특이 항원 표적은 바이러스 발암 유전자 및 네오-항원이다. "네오-항원(neo-antigen)"은 본원에서 게놈-인코딩 단백질의 아미노산 서열을 변경시키는 종양-특이적 돌연변이(tumor-specific mutation)로부터 발생하는 종양 항원으로 이해되어야 한다. 네오-항원은 개개 환자의 암 (또는 신생물 또는 종양)에 고유하게 존재하는 모든, 또는 거의 모든 돌연변이된 네오-항원을 밝히는 전체-게놈 시퀀싱에 의해 확인될 수 있다. 이 돌연변이 네오-항원의 수집은 환자의 암 치료를 위한 개인화된 암 백신의 개발을 위한 항원 소스로서 사용하기 위해 돌연변이된 네오-에피토프의 특이적이고 최적화된 서브셋(subset)을 확인하기 위해 분석될 수 있다. 이러한 네오-항원을 확인하는 방법은 WO2014/168874에 기재되어 있으며, 이는 본원에 참고문헌으로 편입된다.
항원 단백질로부터 "유래된(derived)" 펩타이드는 본원에서 하나 이상의 아미노산의 결실 또는 치환에 의해, N-말단 및/또는 C-말단에서 추가의 아미노산 또는 작용기로 연장에 의해 변형될 수 있는 항원 단백질로부터 선택된 인접 아미노산 서열을 포함하는 것으로 이해되어야 하며, 이는 생체이용률, T-세포에 대한 표적을 향상시키거나, 애주번트 또는 (공동)자극 기능을 제공하는 면역 조절 물질을 포함하거나 방출할 수 있다.
약학 조성물 내에 재구성되거나 및/또는 포함되는 펩타이드는, 비자연적 길이의 합성의 결과로서 또는 펩타이드가 유래되는 단백질로부터 기원하지 않은 추가의 아미노산을 포함하는 결과로서 및/또는 변형된 아미노산 및/또는 비자연적으로 발생하는 아미노산을 포함하는 결과로서, 비자연적으로 발생하는 서열 및/또는 공유결합된 작용기, 예를 들어, 플루오르화기, 플루오로카본기, 인간 톨-유사 리셉터 리간드 및/또는 아고니스트, 올리고뉴클레오타이드 컨주게이트, PSA, 당 사슬 또는 글리칸, pam3cys 및/또는 바람직하게 WO2013051936A1에 기재된 바와 같은 이의 유도체, CpG 올리고데옥시뉴클레오타이드(CpG-ODNs), 시클릭 디뉴클레오타이드(CDNs), DC 펄스 카세트, 테타너스 톡신 유래 펩타이드, 인간 HMGB1 유래 펩타이드를 상술한 바와 같이 펩타이드 내에 또는 펩타이드에 첨부되어 포함하거나 이로 구성될 수 있다. 본 발명의 펩타이드는 2-아미노이소부티르산(Abu, 시스테인의 동배체(isostere)를 포함할 수 있다. 본 발명의 펩타이드의 시스테인은 Abu로 대체될 수 있다.
바람직하게, 본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 펩타이드는 분리된 펩타이드이며, "분리된(isolated)"은 펩타이드가 정제되는 정도를 반영하지 않지만, 펩타이드가 천연 환경으로부터 제거되는(즉, 인간 조작 대상이 되는) 것을 나타내며, 재조합적으로 생산된 펩타이드 또는 합성적으로 생산된 펩타이드일 수 있다.
상대적으로 짧은 펩타이드의 사용은 시험관 내에서 효율적으로 합성될 수 있기 때문에 의약 목적으로 매우 바람직하며, 약 100, 즉 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105 개의 아미노산 보다 큰 네이티브 단백질에는 불가능하거나 비경제적이다. 펩타이드의 화학적 합성은 통상적인 실행이며, 다양한 적합한 방법이 당업자에게 공지되어 있다. 또한, 펩타이드의 화학적 합성은 표준화가 어렵고 광범위한 정제 및 품질 관리 조치가 필요한 손상되지 않은 단백질의 재조합 생산과 관련된 문제를 극복한다. 인간 백혈구 항원(HLA) 클래스 I 및 클래스 II 에피토프(예, 본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 펩타이드에 대해 본원에서 특정된 바와 같은 길이를 갖는)의 길이를 초과하는 길이를 갖는 펩타이드는 특히 WO02/070006에 설명된 바와 같은 전문 항원 제시 세포(APC), 특히 수지상 세포(DC)에 의해 취해지기에 충분히 크고, 함유된 HLA 클래스 I-제시되고 HLA 클래스 II-제시된 에피토프의 세포 표면 제시가 일어나기 전에 DC에서 프로세싱되기 때문에 백신 성분으로서 사용하기에 유리하다. 따라서, (Toes et al., Proc Natl Acad Sci (1996) U S A 93(15):7855, 및 Toes et al., Immunol (1996) 156(10):3911에 나타난 바와 같이) 비-항원 제시 세포에서 최소의 HLA 클래스 I-제시된 에피토프의 전신성 제시에 의한 T 세포 내성의 불리한 유도는 (Zwaveling et al., J. Immunol. (2002) 169:350-358에 나타난 바와 같이) 인간 백혈구 항원(HLA) 클래스 I 및 클래스 II 에피토프의 길이를 초과하는 펩타이드의 적용에 의해 억제된다. 본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 펩타이드에 대해 특정된 길이를 갖는 펩타이드로 백신 접종하는 것과 비교하여, 전장 단백질을 이용한 치료적 백신 접종은 덜 효력이 있을 수 있다(Rosalia et al. Eur. J. Immunol (2013) 43: 2554-2565).
본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 펩타이드는 바람직하게 약 15 내지 약 100 개의 아미노산 길이의 펩타이드이고, 이는 본원에서 또한 긴 펩타이드로 표기되며, 각각은 인간 백혈구 항원(HLA) 클래스 I 및 II 제시된 에피토프의 길이를 초과하며, 이의 단독으로 또는 혼합하여 조합된 CD4+ 및 CD8+ T 세포 반응을 유도하여 환자를 높은 비율로 치료하는데 성공하고 유도한다. 바람직하게, 본 발명의 긴 펩타이드는 긴 합성 펩타이드(synthetic long peptide)(SLPs)로 명명된 합성 펩타이드이다.
"CTL 에피토프"는 본원에서 프로테아좀 매개 단백질분해 절단에 의해 공급원 단백질로부터 유리되고, 이어서 항원 제시 세포(APC), 바람직하게 인간 항원 제시 세포의 세포 표면 상에 HLA 클래스 I 분자에 의해 제시되는 폴리펩타이드 항원의 선형 단편으로 이해된다. 본 발명의 CTL 에피토프는 바람직하게 CD8+ T 세포 반응을 활성화시킬 수 있다. CTL 에피토프는 전형적으로 적어도 8개 내지 최대 12개, 또는 예외적으로 최대 13개 또는 14개의 아미노산을 포함한다. 바람직하게 CTL 에피토프는 8-14개의 아미노산으로 이루어지며, 즉 적어도 8개 내지 최대 14개의 아미노산 길이를 갖는다.
"Th-세포 에피토프"는 본원에서 HLA 클래스 II 분자에 의해 인식되는 선형 펩타이드 단편으로 이해된다. Th 세포 에피토프는 CD4+ T 세포 반응을 유도할 수 있다. HLA 클래스 II-제한 CD4+ T-헬퍼 세포(Th-세포) 에피토프는 전형적으로 15개 내지 최대 20개, 또는 예외적으로 더 많은 아미노산을 포함한다. 바람직하게, HLA 클래스 II-제한 T-헬퍼 세포 에피토프는 10-20개 또는 10-15개의 아미노산을 포함한다.
가장 바람직하게, 본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 펩타이드의 Th-세포 에피토프는 CD4+ T- 헬퍼 메모리 및/또는 CD4+ T-헬퍼 이펙터 반응을 활성화, 즉 CD45RO-양성 CD4+ T-헬퍼 세포의 활성화를 가능하게 한다. 이것은 DC의 CD40-트리거링을 통해 '사멸 허가(license to kill)' 신호(Lanzavecchia (1998) Nature, 393: 413)로 인해 보다 강력한 CD8+ 이펙터 및 메모리 세포독성 T 세포 반응을 이끌 것이다. 다른 환경에서, 활성화된 CD4+ T-헬퍼 세포는 면역계의 비-HLA 제한 킬러 세포를 활성화시킬 수 있다.
본 발명의 문맥에서 "단백질 항원으로부터 최대 100개의 연속적인 아미노산을 포함하는 펩타이드(peptide which comprises at most 100 consecutive amino acids from a protein antigen)"는 단백질 항원으로부터 기원하고 본원에서 정의된 펩타이드에 존재하는 연속적인 아미노산의 수가 100, 99, 98, 97, 96, 95, 94, 93, 92, 91, 90, 89, 88, 87, 86, 85, 84, 83, 82, 81, 80, 79, 78, 77, 76, 75, 74, 73, 72, 71, 70, 69, 68, 67, 66, 65, 64, 63, 62, 61, 60, 59, 58, 57, 56, 55, 54, 53, 52, 51, 50, 49, 48, 47, 46, 45, 44, 43, 42, 41, 40, 39, 38, 37, 36, 35, 34, 33, 32, 31, 또는 30개의 아미노산 또는 그 미만인 것을 의미한다. 본 발명의 문맥에서 "단백질 항원으로부터 적어도 15개의 연속적인 아미노산을 포함하는 펩타이드(peptide which comprises at least 15 consecutive amino acids from a protein antigen)"는 단백질 항원으로부터 기원하고 본원에서 정의된 바와 같은 펩타이드에 존재하는 연속적인 아미노산의 수가 적어도 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45개 또는 그 이상의 아미노산인 것을 의미한다. 본 발명의 문맥에서 "단백질 항원으로부터 15-100개의 연속적인 아미노산을 포함하는 펩타이드(peptide which comprises 15-100 consecutive amino acids from a protein antigen)"는 단백질 항원으로부터 기원하고 본원에서 정의된 바와 같은 펩타이드에 존재하는 연속적인 아미노산의 수가 적어도 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44 또는 45개의 아미노산 및 100, 99, 98, 97, 96, 95, 94, 93, 92, 91, 90, 89, 88, 87, 86, 85, 84, 83, 82, 81, 80, 79, 78, 77, 76, 75, 74, 73, 72, 71, 70, 69, 68, 67, 66, 65, 64, 63, 62, 61, 60, 59, 58, 57, 56, 55, 54, 53, 52, 51, 50, 49, 48, 47, 46, 45, 44, 43, 42, 41, 40, 39, 38, 37, 36, 35, 34, 33, 32, 31, 또는 30개 이하의 아미노산인 것을 의미한다. 보다 바람직하게, 재구성되는 펩타이드 내에 포함되는 단백질 항원으로부터의 인접한 아미노산 서열의 길이는 15-100개 아미노산, 또는 바람직하게는 15-95개 아미노산, 또는 15-90개 아미노산, 또는 15-85개 아미노산, 또는 15-70개 아미노산, 또는 15-25개 아미노산, 또는 15-60개 아미노산, 15-55개 아미노산, 또는 15-50개 아미노산, 더욱 더 바람직하게는 15-45개 아미노산, 더욱 더 바람직하게는 15-40개 아미노산, 더욱 더 바람직하게는 17-39개 아미노산, 보다 더 바람직하게는 19-43개 아미노산, 더욱 더 바람직하게는 22-40개 아미노산, 더욱 더 바람직하게는 28-40개 아미노산 및 더욱 더 바람직하게는 30-39개 아미노산이다.
바람직하게, 본 발명에 따른 약학 조성물은 하기의 특성들 모두를 만족하는 어느 펩타이드를 포함하지 않는다:
a. 염기성 아미노산 잔기의 퍼센트가 산성 아미노산 잔기의 퍼센트와 동일하고, 그리고
b. 소수성 아미노산 잔기의 퍼센트가 48% 이상이다.
이러한 구현의 목적상, 아미노산 잔기는 다음과 같이 "산성", "염기성", "소수성" 또는 "중성"으로 분류된다:
본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 펩타이드는 바람직하게는 항원 펩타이드이다. "항원 펩타이드(antigenic peptides)"는 본원에서 (고도로) 면역원성이며, 대상자, 바람직하게는 인간 또는 동물 대상자에 백신 조성물로서 투여될 경우에 강력한 결합된 항원-유도 CD4+ T 헬퍼 및 CD8+ 세포독성 T 세포 반응을 유도할 수 있는 것으로 이해되어야 한다. 상기 펩타이드는 면역원성일 것으로 예측될 수 있고 및/또는 시험관 내 또는 생체 외 분석법을 사용하여 또는 면역원성을 확립하기 위해 당업계에서 인정된 생체 내 시험을 수행하여 면역원성인 것으로 입증될 수 있다. 바람직하게, 펩타이드는 대상자에서, 바람직하게는 하기에 의해 검출가능한 바와 같이, 항원 관련 질병 또는 컨디션의 예방, 부분적 클리어런스 및/또는 치료 또는 완전한 클리어런스에 효과적으로 사용될 수 있다:
- Elispot 분석 또는 CD4+ 또는 CD8+ T-세포의 테트라머 염색에 의해 확립된 면역계의 활성화 또는 유도 및/또는 말초 혈액 또는 조직 내 항원 특이적 활성화 CD4+ 및/또는 CD8+ T-세포의 증가 또는 1주에 적어도 1회의 처리 후 유세포 분석시 CD4+ 및 CD8+ T 세포의 세포 내 사이토카인 염색에 의해 확립된 이들 T-세포에 의해 생성된 사이토카인의 증가; 및/또는
- 항원 관련 감염의 증식 또는 항원 발현 세포의 검출 가능한 질병의 억제 또는 항원 발현 세포의 세포 생존성의 감소; 및/또는
- 항원 발현 세포의 세포 사멸의 유도 또는 증가된 유도; 및/또는
- 항원 발현 세포의 증가의 억제 또는 예방.
바람직한 구현으로, 본 발명의 백신 조성물은 펩타이드의 조합을 포함하며, 여기서 펩타이드의 조합은 치료할 인간 대상자의 집단에서 우세한 HLA 대립 유전자에 의해 인코딩된 HLA 클래스 I 분자를 적어도 70%, 80%, 90%, 92%, 94%, 95%, 96%, 97%, 98%, 99% 또는 100%를 포함한다. 치료할 인간 대상자의 집단에서 우세한 HLA 대립 유전자. 본 발명에 따른 펩타이드에서 바람직한 HLA 클래스 I 에피토프는 다음과 바인딩할 수 있는 에피토프이다: HLA-A0101; HLA-A0201; HLA-A0206; HLA-A0301; HLA-A1101; HLAA2301; HLA-A2402; HLA-A2501; HLA-A2601; HLA-A2902; HLA-A3001; HLAA3002; HLA-A3101; HLA-A3201; HLA-A3303; HLA-A6801; HLA-A6802; HLAA7401; HLA-B0702; HLA-B0801; HLA-B1301; HLA-B1302; HLA-B1402; HLAB1501; HLA-B1502; HLA-B1525; HLA-B1801; HLA-B2702; HLA-B2705; HLAB3501; HLA-B3503; HLA-B3701; HLA-B3801; HLA-B3901; HLA-B4001; HLAB4002; HLA-B4402; HLA-B4403; HLA-B4601; HLA-B4801; HLA-B4901; HLAB5001; HLA-B5101; HLA-B5201; HLA-B5301; HLA-B5501; HLA-B5601; HLAB5701; HLA-B5801 및 HLA-B5802. 바람직한 구현으로, 본 발명의 펩타이드는 치료할 인간 대상자의 집단에서 우세한 HLA 대립 유전자에 의해 인코딩된 HLA 클래스 I 분자를 적어도 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 또는 100% 포함하며, 여기서 "HLA 클래스 I 분자를 포함"한다는 것은 본원에서 상기 HLA 클래스 I 분자에 대한 바인딩 친화력, 바람직하게는 중간 바인딩 친화력, 보다 바람직하게는 높은 바인딩 친화력을 나타내는 CTL 에피토프를 포함하는 것으로 이해된다. 바람직하게, 본 발명의 펩타이드는 다음으로 구성된 HLA 클래스 I 분자 그룹의 적어도 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% 또는 100%를 포함한다: HLA-A0101; HLA-A0201; HLA-A0206; HLA-A0301; HLA-A1101; HLA-A2301; HLA-A2402; HLA-A2501; HLA-A2601; HLA-A2902; HLA-A3001; HLA-A3002; HLA-A3101; HLA-A3201; HLA-A3303; HLA-A6801; HLA-A6802; HLA-A7401; HLA-B0702; HLA-B0801; HLA-B1301; HLA-B1302; HLA-B1402; HLA-B1501; HLA-B1502; HLA-B1525; HLA-B1801; HLA-B2702; HLA-B2705; HLA-B3501; HLA-B3503; HLA-B3701; HLA-B3801; HLA-B3901; HLA-B4001; HLA-B4002; HLA-B4402; HLA-B4403; HLA-B4601; HLA-B4801; HLA-B4901; HLA-B5001; HLA-B5101; HLA-B5201; HLA-B5301; HLA-B5501; HLA-B5601; HLA-B5701; HLA-B5801 및 HLA-B5802.
재구성 조성물은 단일 타입의 펩타이드(즉, 모두 실질적으로 동일한 아미노산 서열을 갖거나, 또는 동일한 아미노산 서열을 갖는)을 재구성하기 위해 또는 상이한 아미노산 서열을 갖는 상이한 펩타이드의 혼합물을 재구성하는데 사용될 수 있다. 본 발명의 약학 조성물은 바람직하게 적어도 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32개 및 최대 33개의 상이한 펩타이드를 포함한다. "상이한 펩타이드(different peptides)"는 상이한 아미노산 서열을 가지며, 바람직하게는 이의 전체 길이에 걸쳐 결정되는 바와 같이, 60%, 50%, 40% 미만 또는 바람직하게는 30% 미만의 서열 동일성을 갖는 것으로 본원에서 이해되어야 한다. 본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 상이한 펩타이드는 이들 펩타이드가 유래된 단백질 항원의 전체 아미노산 서열과 함께 중첩되는 상기 정의된 길이를 갖는 펩타이드일 수 있다. 그러나, 일부 경우에는 전장 단백질 항원에 걸친 중복(합성)의 긴 펩타이드의 완전한 세트로 면역화하는 것은 실현가능하지 않으며, 선택이 이루어져야 할 필요가 있다. 백신에서 펩타이드의 수를 줄이기 위해, 바람직하게 가장 높은 백분율의 환자에 의해 인식되는 가장 높은 면역원성의 긴 펩타이드가 선택되고 포함된다.
본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 펩타이드들 중 적어도 하나는 분자간 디설파이드 결합이 가능한 적어도 하나의 시스테인 잔기를 가질 수 있거나, 또는 분자내 및 분자간에 디설파이드 결합 형성이 가능한 적어도 2개의 시스테인 잔기를 가질 수 있다. 바람직하게, 본 발명에 따른 백신 조성물은 본원에서 상기 정의된 바와 같이 치료할 인간 대상자의 집단에서 우세한 HLA 대립 유전자에 의해 인코딩된 HLA 클래스 I 분자를 적어도 70%, 80%, 90%, 92%, 94%, 95%, 96%, 97%, 98%, 99% 또는 100%를 포함한다.
본 발명의 재구성 조성물 내에 재구성되는 펩타이드의 양은 바람직하게 본원에서 상기 정의된 바와 같이 단일 용량으로 주입되는 약학적 투여 단위 및/또는 양이다.
건조된 펩타이드는 추가 성분이 없는 펩타이드일 수 있으나, 트리플루오르 아세트산(TFA)과 같은 버퍼 성분, 소듐, 포타슘 또는 포스페이트염(예, NaCl, KCl 및 NaPO4)과 같은 염을 또한 포함할 수 있다. 추가 성분의 양은 바람직하게는 재구성되는 건조 펩타이드의 총 중량의 30% 미만, 보다 바람직하게는 25% 미만이다. 재구성되는 건조된 펩타이드는 이에 한정하는 것은 아니나, 로터 증발, 동결 건조(프리즈 드라잉) 및 분무 건조와 같은 공정에 의해 수득될 수 있는 물리적 건조 상태일 수 있다.
본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 펩타이드가 유도되는 바람직한 단백질 항원은 하기에 정의된다.
HPV-유래 펩타이드
본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 펩타이드는 초기 HPV 항원 단백질 E2, E6 또는 E7로부터 유래된 펩타이드(의 혼합물)일 수 있다. 바람직하게, 인접 아미노산 서열은 혈청형 16, 18, 31, 33 또는 45와 같은 고위험 HPV 혈청형으로부터의 HPV E6 및 E7 단백질의 전장 아미노산 서열, 보다 바람직하게는 HPV E6 및 E7 혈청형 16, 18, 31 또는 33, 가장 바람직하게는 혈청형 16 또는 18로부터의 아미노산 서열로부터 선택되며, 그 중 16이 가장 바람직하다. HPV 혈청형 16 E2(UniProtKB-P03120), E6(UniProtKB-P03126) 및 E7(UniProtKB-P03129) 단백질의 아미노산 서열을 각각 SEQ ID NO: 14-16에 나타내었다. HPV 혈청형 18 E2(UniProtKB-P06790), E6(UniProtKB-P06463) 및 E7(UniProtKB-P06788) 단백질의 아미노산 서열을 각각 SEQ ID NO: 17-19에 나타내었다.
본 발명의 약학 조성물 내에 재구성 및/또는 포함되고 HPV E6 및 E7 단백질로부터 유래된 바람직한 펩타이드 및 펩타이드 혼합물은 WO00/75336 A2에 정의된 바와 같다. 바람직한 펩타이드는 SEQ ID NO: 20-26 중 어느 하나에 의해 나타낸 면역원성 영역 내에 인접한 서열을 포함하거나 이로부터 구성된 펩타이드이다.
바람직하게, 본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 하나 이상의 펩타이드는 SEQ ID NO: 27-67로 나타낸 그룹으로부터 선택된 CTL 에피토프를 포함한다.
본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되고 HPV E2, E6 및 E7 단백질로부터 유래된 바람직한 펩타이드 및 펩타이드 혼합물은 본원에 참고문헌으로 편입된, WO2002/070006 A2 및 WO2002/090382에 정의된 바와 같다. 바람직한 펩티드는 하기 HPV 면역원성 영역 E2(31-120); E2(151-195); E2(271-365); E6(81158); E7(31-77) 내에 인접한 서열을 포함하거나 이로 구성되는 펩타이드이며, 바람직하게는 HPV 16 혈청형이고 본원에서 각각 SEQ ID NO: 68-72로 정의된다.
바람직하게, 본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 하나 이상의 펩타이드는 DR1/E2 351-365, DR2/E2 316-330, DR2/E2 346-355, DR4/E2 51-70, E2 61-76, DQ6/E2 311-325, DR15/E7 50-62, DR3/E7 43-77, DQ2/E7 35-50 및 DR1/E6 127-142(본원에서 각각 SEQ ID NO: 73-82로 나타냄)로부터 선택된 Th 에피토프를 포함한다.
바람직하게, 본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 펩타이드는 자궁 경부 종양 병변에 침윤하는 T 세포에 의해 또는 자궁 경부 종양 병변으로부터 배출되는 골반 영역의 림프절에 존재하거나 이로부터 분리된 T 세포에 의해 인식되는 적어도 하나의 T 세포 에피토프를 포함한다. 바람직하게, T 세포 에피토프는 전이성 종양 세포를 포함하는 배수 림프절에 존재하거나 이로부터 분리된다. 이러한 에피토프는 예를 들어, 본원에 참고문헌으로 편입된 WO2008/147187 Al, US20060182762A1, WO2006013336A1, WO2009148230A2, WO2009148229A2, WO2002044384A2에 개시되어있다.
본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 바람직한 펩타이드에서, 인접 아미노산 서열은, 자궁 경부 종양 병변에 침윤하는 T 세포에 의해 또는 배수 림프절의 T 세포에 의해 인식되는 T-세포 에피토프인 것으로 입증된, SEQ ID NO: 83-104로 나타낸 아미노산 서열로 구성되는 그룹으로부터 선택된 인접 아미노산 서열로 구성되는 그룹으로부터 선택된 에피토프를 포함한다.
본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 펩타이드에 포함된 바람직한 클래스 II CD4+ Th 세포 에피토프는 SEQ ID NO: 83-99로 나타낸 아미노산 서열로 구성되는 그룹으로부터 선택된 인접 아미노산 서열로 구성되는 그룹으로부터 선택된다.
본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 펩타이드에 포함된 바람직한 클래스 I CD8+ CTL 세포 에피토프는 SEQ ID NO: 85, 82, 100-104로 나타낸 아미노산 서열로 구성되는 그룹으로부터 선택된 인접 아미노산 서열로 구성되는 그룹으로부터 선택된다.
본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 바람직한 펩타이드는 SEQ ID NO: 1-13으로 나타낸 아미노산 서열로 구성되는 그룹으로부터 선택된 인접 아미노산 서열을 포함하거나 이로 구성된다.
본 발명의 백신 조성물 내에 재구성되거나 및/또는 포함되는 펩타이드의 바람직한 혼합물은 SEQ ID NO: 1-5로부터 선택된 서열을 포함하거나 이로부터 구성된 펩타이드 중 적어도 1, 2, 3, 4 또는 5개; SEQ ID NO: 1-6으로부터 선택된 인접 아미노산 서열을 포함하거나 이로부터 구성된 펩타이드 중 적어도 1, 2, 3, 4, 5 또는 6개; 그리고 SEQ ID NO: 7-13으로 나타낸 아미노산 서열로 구성되는 그룹으로부터 선택된 인접 아미노산 서열을 포함하거나 또는 이로 구성되는 펩타이드 중 적어도 1, 2, 3, 4, 5, 6 또는 7개를 갖는 펩타이드의 혼합물이다. 바람직하게, 약학 조성물은 SEQ ID NO: 1-5 또는 SEQ ID NO: 1-6 또는 SEQ ID NO: 7-13 서열을 갖는 펩타이드의 혼합물을 포함한다. 바람직하게, 혼합물 중의 상이한 펩타이드는 약학 조성물에 실질적으로 동일한 비율로 존재한다.
HBV-유래 펩타이드
본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 펩타이드는 다양한 유전형, 예를 들어, 본원에서 SEQ ID NO: 105-108로 나타낸, HBV-A 단백질, HBV 폴리머라아제(UniProtKB - P03159), HBV 코어 단백질(UniProtKB - P0C625), HBV X 단백질, 및 HBV 라지 표면 단백질(UniProtKB - P03141)로부터 유래된 펩타이드(의 혼합물)일 수 있다. 이들 펩타이드 내에 존재하는 바람직한 펩타이드, 펩타이드 혼합물 및 에피토프는 예를 들어, 본원에서 참고문헌으로 편입된, WO2015/187009, WO2014/102540 A1, WO 93/03753, WO 95/03777, US2010/0068228A1, US2009/0311283 A1에 기술되어있다.
본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 바람직한, 하나 이상의 펩타이드는 SEQ ID NO: 109-146로 구성되는 그룹으로부터 선택된 아미노산 서열을 포함하거나 이로 구성된다.
바람직하게, 본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 펩타이드는 SEQ ID NO: 109, 113, 118, 121, 122, 126, 129, 132, 133, 134, 135, 138 및 142으로 구성되는 그룹으로부터 선택된, 보다 바람직하게 SEQ ID NO: 109, 113, 118, 121, 122, 126, 129, 132, 133, 135, 138 및 142로 구성되는 그룹으로부터 선택된, 보다 바람직하게 SEQ ID NO: 113, 118, 121, 122, 126, 129, 132, 133, 134, 135 및 142로 구성되는 그룹으로부터 선택된, 보다 바람직하게 SEQ ID NO: 113, 118, 121, 122, 126, 129, 132, 133, 135 및 142로 구성되는 그룹으로부터 선택된, 보다 바람직하게 SEQ ID NO: 118, 121, 129, 132, 133 및 142로 구성되는 그룹으로부터 선택된, 보다 바람직하게 SEQ ID NO: 133, 142 및 121로 구성되는 그룹으로부터 선택된 펩타이드를 포함하거나 이로 구성된다. 본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 하나 이상의 펩타이드는 SEQ ID NO: 122, 129 및 133으로 구성되는 그룹으로부터 선택된 펩타이드를 포함하거나 이로 구성된다.
본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 펩타이드의 바람직한 혼합물은 SEQ ID NO: 109-146으로 구성되는 그룹으로부터 선택된, 보다 바람직하게 SEQ ID NO: 109, 113, 118, 121, 122, 126, 129, 132, 133, 134, 135, 138 및 142로 구성되는 그룹으로부터 선택된, 보다 바람직하게 SEQ ID NO: 109, 113, 118, 121, 122, 126, 129, 132, 133, 135, 138 및 142로 구성되는 그룹으로부터 선택된, 보다 바람직하게 SEQ ID NO: 113, 118, 121, 122, 126, 129, 132, 133, 134, 135 및 142로 구성되는 그룹으로부터 선택된, 보다 바람직하게 SEQ ID NO: 113, 118, 121, 122, 126, 129, 132, 133, 135 및 142로 구성되는 그룹으로부터 선택된, 보다 바람직하게 SEQ ID NO: 118, 121, 129, 132, 133 및 142로 구성되는 그룹으로부터 선택된, 가장 바람직하게 SEQ ID NO: 133, 142 및 121로 구성되는 그룹으로부터 선택된 펩타이드로 구성되거나 이를 포함하는 펩타이드들의 적어도 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32개 및 최대 33개의 상이한 펩타이드들의 혼합물이다. 보다 바람직한 조성물은 SEQ ID NO: 109, 118, 121, 122, 126, 129, 132-135로 구성되는 그룹으로부터 선택된, 보다 바람직하게 SEQ ID NO: 121, 129 및 133으로 구성되는 그룹으로부터 선택된 펩타이드로 구성되거나 이를 포함하는 펩타이드들의 적어도 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32개 및 최대 33개의 상이한 펩타이드들을 포함하는 것이다. 본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 보다 바람직한 혼합물은 SEQ ID NO: 139, 140, 133, 139, 142, 118, 129 중 적어도 하나를 포함하거나 이로 구성되는 펩타이드와 함께 SEQ ID NO: 121의 펩타이드를 포함하거나 이로 구성되는 펩타이드를 포함하는 혼합물; 및 SEQ ID NO: 139, 140, 63, 139, 142, 118, 129를 포함하거나 또는 이로 구성되는 펩타이드와 함께 SEQ ID NO: 133의 펩타이드를 포함하거나 이로 구성되는 펩타이드를 포함하는 혼합물이다. 바람직하게, 혼합물 중의 상이한 펩타이드는 약학 조성물에 실질적으로 동일한 비율로 존재한다.
PRAME-유래 펩타이드
본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 펩타이드는 본원에서 SEQ ID NO: 147로 나타낸 PRAME(UniProtKB - P78395)으로부터 유래된 펩타이드(의 혼합물)일 수 있다. 이들 펩타이드 내에 존재하는 바람직한 펩타이드, 펩타이드 혼합물 및 에피토프는 예를 들어, 본원에 참고문헌으로 편입된 WO 2008/118017 A2에 개시되어 있다. 바람직하게, 재구성되는 하나 이상의 펩타이드는 SEQ ID NO: 148-167로 정의된 아미노산 서열로 구성되는 그룹으로부터 선택된 펩타이드를 포함하거나 이로 구성된다. 본 발명의 백신 조성물 내에 재구성되거나 및/또는 포함되는 펩타이드의 바람직한 혼합물은 SEQ ID NO: 148-167로부터 선택된 적어도 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19 또는 20개의 상이한 펩타이드의 혼합물이다.
바람직하게, 본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 하나 이상의 펩타이드는 SEQ ID NO: 168-169로부터 선택된 Th 에피토프를 포함한다.
P53-유래 펩타이드
본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 펩타이드는 본원에서 SEQ ID NO: 190으로 나타낸 P53(예, UniprotKB P04637)로부터 유래된 펩타이드(의 혼합물)일 수 있다. 이들 펩타이드 내에 존재하는 바람직한 펩타이드, 펩타이드 혼합물 및 에피토프는 예를 들어, 본원에 참고문헌으로 편입된 WO 2008/147186 A2에 개시되어 있다. 바람직하게, 재구성되는 하나 이상의 펩타이드는 SEQ ID NO: 191-211로 정의된 아미노산 서열로 구성되는 그룹으로부터 선택된, 바람직하게는 SEQ ID NO: 191-204로 정의된 아미노산 서열로 구성되는 그룹으로부터 선택된 펩타이드를 포함하거나 이로 구성된다.
본 발명의 백신 조성물 내에 재구성되거나 및/또는 포함되는 펩타이드의 바람직한 혼합물은 SEQ ID NO: 191-211로부터 선택된 적어도 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19 또는 20개의 상이한 펩타이드의 혼합물이다.
PSMA-유래 펩타이드
본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 펩타이드는 본원에서 SEQ ID NO: 212로 나타낸 PSMA(예, UniprotKB Q04609)로부터 유래된 펩타이드(의 혼합물)일 수 있다. 이들 펩타이드 내에 존재하는 바람직한 펩타이드, 펩타이드 혼합물 및 에피토프는 예를 들어, 본원에 참고문헌으로 편입된 WO 2013/006050 A1에 개시되어 있다. 바람직하게, 재구성되는 하나 이상의 펩타이드는 SEQ ID NO: 213-232로 정의된 아미노산 서열로 구성되는 그룹으로부터 선택된 펩타이드를 포함하거나 이로 구성된다.
본 발명의 백신 조성물 내에 재구성되거나 및/또는 포함되는 펩타이드의 바람직한 혼합물은 SEQ ID NO: 213-232로부터 선택된 적어도 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19 또는 20개의 상이한 펩타이드의 혼합물이다.
또한 내부에 포함되는 바람직한 항원 단백질, 재구성되는 펩타이드 및 이들 펩타이드 내의 에피토프는 본원에서 정의된 특정 항원 단백질, 펩타이드 및 에피토프 중 어느 것과 실질적으로 동일성을 나타내는 항원 단백질, 펩타이드 및 에피토프이다. 서열 동일성은 서열을 비교함으로써 결정되는 바와 같이, 2개 이상의 아미노산 서열(폴리펩타이드 또는 단백질) 사이의 관계로서 본원에서 정의된다. 당해 기술 분야에서, "동일성(identity)"은 또한 이러한 서열의 스트링 사이의 일치에 의해 결정된 아미노산 서열 간의 서열 관련성의 정도를 의미한다. 서열 동일성은 두 서열의 길이에 따라 전역 또는 국소 정렬 알고리즘을 사용하여 두 펩타이드 서열의 정렬에 의해 결정될 수 있다. 유사한 길이의 서열은 전체 길이에 걸쳐 서열을 최적으로 정렬하는 전역 정렬 알고리즘(예, Needleman Wunsch)을 사용하여 정렬되는 것이 바람직하지만, 실질적으로 상이한 길이의 서열은 국소 정렬 알고리즘(예, Smith Waterman)을 사용하여 정렬되는 것이 바람직하다. 이어서, 서열(예를 들어, 디폴트 파라미터를 사용하여 프로그램 GAP 또는 BESTFIT에 의해 최적으로 정렬된 경우)이 적어도 서열 동일성(하기 정의된 바와 같음)의 적어도 특정 최소의 퍼센트를 공유하는 경우에, 서열은 "실질적으로 동일하다(substantially identical)"라고 언급될 수 있다. GAP는 Needleman 및 Wunsch 전역 정렬 알고리즘을 사용하여 이들의 전체 길이(전장)에 걸쳐 두 개의 서열을 정렬하여, 일치의 수를 최대화하고, 갭의 수를 최소화한다. 두 서열이 유사한 길이를 가질 때 서열 동일성을 결정하는데 전역 정렬이 적절하게 사용된다. 일반적으로, 갭 생성 패널티 = 50(뉴클레오티드)/8(단백질) 및 갭 확장 패널티 = 3(뉴클레오티드)/2(단백질)로 GAP 디폴트 파라미터가 사용된다. 단백질에 대한 디폴트 스코어링 매트릭스는 Blosum62 (Henikoff & Henikoff, 1992, PNAS 89, 915-919)이다. 퍼센트 서열 동일성에 대한 서열 정렬 및 스코어는 GCG Wisconsin Package, Version 10.3(Accelrys Inc., 9685 Scranton Road, San Diego, CA 92121-3752 USA으로부터 구입가능함)과 같은 컴퓨터 프로그램을 사용하여, 또는 상기 GAP에 대해서와 동일한 파라미터를 사용하거나 또는 디폴트 설정을 사용하는('니들(needle)'과 '워터(water)' 모두에 대한 디폴트 갭 스코어링 패널티는 10.0이고, 디폴트 갭 확장 패널티는 0.5이며; 디폴트 스코어링 매트릭스는 단백질에 대해 are Blossum62임) 프로그램 "니들(needle)"(전역 Needleman Wunsch 알고리즘을 사용함) 또는 EmbossWIN version 2.10.0의 "워터(water)"(국소 Smith Waterman 알고리즘을 사용함)와 같은 오픈 소스 소프트웨어를 사용하여 결정될 수 있다. 서열이 실질적으로 상이한 전체 길이를 갖는 경우, Smith Waterman 알고리즘을 사용하는 것과 같은 국소 정렬이 바람직하다.
대안적으로, 퍼센트 동일성은 FASTA, BLAST 등과 같은 알고리즘을 사용하여 공개 데이터베이스를 서치함으로써 결정될 수 있다. 따라서, 본 발명의 단백질 서열은, 예를 들어, 다른 계열 멤버나 관련 서열을 확인하기 위해 공개 데이터베이스에 대한 서치를 수행하는 "쿼리 서열(query sequence)"로서 추가로 사용될 수 있다. 이러한 서치는 문헌 [Altschul, et al. (1990) J. Mol. Biol. 215:403-10.]의 BLASTp 및 BLASTx 프로그램(버전 2.0)을 사용하여 수행될 수 있다. 본 발명의 단백질 분자와 상동인 아미노산 서열을 얻기 위해 BLASTx 프로그램, 스코어 = 50, 워드길이 = 3으로 BLAST 단백질 서치를 수행할 수 있다. 비교 목적으로 갭 정렬을 얻기 위해, Gapped BLAST는 문헌 [Altschul et al., (1997) Nucleic Acids Res. 25(17): 3389-3402]에 기재된 바와 같이 이용될 수 있다. BLAST 및 Gapped BLAST 프로그램을 이용할 경우, 각각의 프로그램의 디폴트 파라미터(예, BLASTx 및 BLASTp)를 사용할 수 있다. http://www.ncbi.nlm.nih.gov/에서 생명공학 정보 국립 센터(National Center for Biotechnology Information)의 홈페이지를 참조바람.
본원에서 정의된 관련 항원 단백질, 펩타이드 또는 에피토프에 대한 실질적인 동일성을 나타내는 항원 단백질, 펩티드 또는 에피토프는 본원에서 상기 특정 서열의 전체 길이에 기초하여(즉, 이의 전체 길이에 걸쳐 또는 전체로서), 본원에 언급된 특정 서열들 중 어느 하나와 적어도 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 또는 99% 동일성을 갖는 것으로 이해되어야 한다.
의약 용도
지속 감염(persistent infection) 또는 만성 감염, 전암성 질병 및/또는 암을 예방 또는 치료하는 방법이 제공된다. 즉, 지속 감염 또는 만성 감염, 전암성 질병 및/또는 암의 예방 또는 치료를 위한 의약으로서 사용하기 위한 상기 본원에서 정의된 바와 같은 본 발명의 약학 조성물이 제공된다. 이러한 방법 또는 사용은 본 발명의 약학 조성물을 예방 및/또는 치료가 필요한 대상자에게 투여하는 단계를 포함한다. 예방 및/또는 치료를 필요로 하는 대상자는 또한 환자로 언급될 수 있으며, 이에 한정하는 것은 아니나, 인간 또는 비인간 포유 동물, 예를 들어 비-인간 영장류, 소, 말, 개, 양, 또는 고양이과를 포함하는 포유 동물과 같은 동물을 지칭할 수 있다.
바람직하게, 본원에서 상기 정의된 바와 같은 약학적 투여 단위가 제공된다. 또한 전술한 바와 같이, 상기 약학적 투여 단위는 단일 샷으로 한번 또는 다른 위치에 투여되는 다중 용량으로 주어질 수 있다. 예를 들어, 약학적 투여 단위는 치료할 대상자의 두 다리 또는 팔 중 하나에 각각 투여되는 투 샷으로 나누어질 수 있다. 투 샷은 동일하거나 상이한 펩타이드 혼합물을 포함할 수 있다. 예를 들어, 제1샷은 SEQ ID NO: 1-5 또는 SEQ ID NO: 1-6 을 포함할 수 있고, 제2샷은 SEQ ID NOs 7-13을 포함할 수 있으며, 두가지 샷 모두 단일 또는 실질적으로 단일 시점에서 투여되고, 여기서 실질적으로 단일 시점은 최대 약 15분 이내, 바람직하게는 최대 2분 이내로 이해되어야 한다.
단일 또는 다중 샷의 투여는, 이에 한정하는 것은 아니나, 매일, 1주에 2회, 매주, 2주에 1회, 3주에 1회, 4주에 1회, 5주에 1회, 6주에 1회, 매월 1회, 2개월에 1회, 3개월에 1회, 4개월에 1회, 5개월에 1회, 6개월에 1회, 7개월에 1회, 8개월에 1회, 1년에 1회, 2년에 1회, 5년에 1회 또는 10년에 1회와 같이, 한번에 수행되거나 또는 택일적으로 후속적으로 반복될 수 있다.
바람직하게, 약학 조성물은 본원에서 상기 정의된 바와 같은 유효량으로 투여된다. 바람직하게, 본 발명의 약학 조성물은, 점막 투여 또는 피부 내 및/또는 피내 투여 또는 종양 내 투여와 같은 다른 투여 경로가 예상될 수 있지만, 예를 들어 주사에 의한 것과 같이 정맥 내 또는 피하, 또는 근육 내 투여용이다. 본 발명의 약학 조성물은 단일 투여로 투여될 수 있다. 대안적으로, 투여는 필요하다면 반복될 수 있고 및/또는 별개의 펩타이드 또는 펩타이드 혼합물 또는 상이한 펩타이드 또는 펩타이드 혼합물을 포함하는 조성물이 연속적으로 투여될 수 있으며, 여기서 연속적으로는 시간 및/또는 위치적으로 이루어질 수 있다.
바람직하게, 약학 조성물은 펩타이드에 포함되는 적어도 하나의 에피토프에 대해 T 세포 반응을 유도하기 위한 백신 조성물이다. 바람직하게, 백신은 예를 들어, 지속 감염, 암성(신형성) 또는 전암성 질병, 바람직하게는 하기에 의해 검출가능한 바와 같이, 항원 관련 질병 또는 컨디션의 예방, 부분적 클리어런스 및/또는 치료 또는 완전한 클리어런스를 위한 것이다:
- Elispot 분석 또는 CD4+ 또는 CD8+ T-세포의 테트라머 염색에 의해 확립된 면역계의 활성화 또는 유도 및/또는 말초 혈액 또는 조직 내 항원 특이적 활성화 CD4+ 및/또는 CD8+ T-세포의 증가 또는 1주에 적어도 1회의 처리 후 유세포 분석시 CD4+ 및 CD8+ T 세포의 세포 내 사이토카인 염색에 의해 확립된 이들 T-세포에 의해 생성된 사이토카인의 증가; 및/또는
- 항원 관련 감염의 증식 또는 항원 발현 세포의 검출 가능한 질병의 억제 또는 항원 발현 세포의 세포 생존성의 감소; 및/또는
- 항원 발현 세포의 세포 사멸의 유도 또는 증가된 유도; 및/또는
- 항원 발현 세포의 증가의 억제 또는 예방.
본 발명의 방법을 통해 예방 및/또는 치료되는 암의 예는 이에 한정하는 것은 아니나, 자궁경부 상피내 종양(CIN), 외음부 상피내 종양(VIN), 질 상피내 종양(VaIN), 항문 상피내 종양(AIN), 및 패널(penal) 상피내 종양(PIN)뿐만 아니라, 자궁 경부, 외음부, 질, 항문, 페니스, 호흡소화관, 및 두경부의 암; 간암, 백혈병(예, 급성 백혈병, 급성 림프구성 백혈병, 급성 골수구성 백혈병(acute myelocytic leukemia), 급성 골수아구성 백혈병(acute myeloblastic leukemia), 급성 전골수구성 백혈병, 급성 골수단핵구 백혈병, 급성 단핵구 백혈병, 급성 적혈구 빈혈, 만성 백혈병, 만성 골수구성 백혈병, 만성 림프구성 백혈병), 다혈성 빈혈, 림프종(예, 호지킨병, 비호지킨병), 월 데스트롬의 거대글로불린혈증, 헤비 체인 질병(heavy chain disease), 및 육종 및 암종과 같은 고형 종양(섬유 육종, 점액 육종, 지방 육종, 연골 육종, 골원성 육종, 척색종, 혈관 육종, 내피 육종, 림프관 육종, 림프안지오엔도텔리오사코마(lymphangioendotheliosarcoma), 윤활막종, 중피종, 유잉 종양, 평활근 육종, 횡문근 육종, 결장암, 췌장암, 유방암, 난소암, 전립선암, 편평세포 암종, 기저세포 암종, 선암종, 피지선 암종, 유두암, 유두 선암종, 낭성 암종, 수질 암종, 기관지암종, 신장 세포 암종, 간세포암, 담관 암종, 융모암종, 정상피종, 배아암종, 윌름 종양, 자궁암, 고환암, 폐암, 소세포 폐암, 비소세포 폐암종, 방광암종, 다발성 골수종, 상피암종, 신경교종, 성상세포종, 수모세포종, 두개인두종, 뇌교종, 송과체종, 혈관모세포종, 청신경종, 피지교종, 슈반세포종, 수막종, 흑색종, 신경모세포종 및 망막모세포종)을 포함한다.
본 발명의 방법은 별도의 치료로서 제공되거나 본 발명의 약학 조성물에 첨가 될 수 있는 병용 요법의 일부일 수 있다. 본 발명의 방법은 관문 조절 차단체(checkpoint control blockers), 선택된 TNF 리셉터계 멤버들(예, CD40, 4-1BB/CD137, OX-40/CD134 및 CD27)을 표적으로 하는 모노클로날 항체, 면역 억제성 사이토카인(예, IL-10, TGF-β 및 IL-6) 및/또는 γC 사이토카인(예, IL-7, IL-15 및 IL-21 또는 IL-2), IDO(인돌레아민 2,3-디옥시게나아제) 인히비터, 탈리도마이드(thalidomide) 및/또는 이의 유도체, 추가 면역 조절제(예, 면역억제 Tregs 및/또는 MDSCs를 고갈시키는 것으로 알려진 화합물), 케어 치로의 스탠다드, 예, 화학치료, 방사성 치료, 수술, IFN-α 컨디셔닝, 항바이러스 요법, 항균 요법, UV 요법, 항염증제 요법 등과 조합될 수 있다. 전암성 질병 또는 암의 치료 또는 예방의 경우에, 펩타이드-기반 백신은 방사성 치료 및/또는 카보플라틴, 파클리탁셀, CarboTaxol(카보플라틴, 파클리탁셀의 조합) 및/또는 시스플라틴을 이용한 치료와 같은 화학적 치료와 조합될 수 있다. 예를 들어, 본 발명의 방법은 화학적 치료가 3주에 1회 적용되는 화학 치료 요법의 일부일 수 있다. 바람직하게는, 본 발명의 약적 조성물의 제1 약학적 투여 단위는 화학 치료의 제2 또는 제3 사이클 후 2 주에 투여된다.
재구성 방법
또한, 다음의 후속 단계를 포함하는, 건조된, 바람직하게는 동결 건조된 펩타이드를 재구성하는 방법이 제공된다:
a) 건조되고, 바람직하게는 동결 건조된 펩티드를 포함하는 바이얼을 제공하는 단계;
b) 상기 펩타이드를 해동, 바람직하게는 약 5 내지 30분 동안 해동시키는 단계;
c) 본 발명의 재구성 조성물을 상기 펩타이드를 포함하는 바이얼에, 바람직하게는 상기 바이얼을 스월링(swirling) 하지 않고, 첨가하는 단계;
d) 혼합, 바람직하게는 약 0.5-5분 동안 혼합시키는 단계; 및
e) 투명한 용액이 수득될 때까지, 바람직하게는 약 1-3분 동안 스월링(swirling) 하는 단계.
바람직하게, 단계 b) 내지 e)는 실온에서 수행된다.
또한,
(i) 제1 주사기에서 상기 정의된 건조된 펩타이드를 재구성하는 방법에 의해 수득가능한 재구성된 펩티드를 수집하는 단계;
(ii) 단계 (i)의 제1 주사기를 커넥터를 사용하여 오일-기반 애주번트를 포함하는 제2 주사기에 연결하는 단계;
(iii) 제1 주사기의 내용물을 제2 주사기로 밀어 넣고 거꾸로 당기는(backwards) 단계;
(iv) 단계 (iii)을 약 10-50초 내에 총 10-50회 반복하는 단계
의 후속 단계를 포함하는 약학 조성물 제조방법이 제공된다.
바람직하게, 단계 (i) 내지 (iv)가 실온에서 수행된다.
건조된 펩타이드를 재구성하는 방법에서 단계 e)에서 수득된 투명한 용액은 출발 물질로서, 즉 약학 조성물 제조 방법의 단계 (i)에서 "재구성된 펩타이드"로서 사용될 수 있는 재구성된 펩타이드를 포함하는 재구성 조성물로 이해되어야 한다.
바람직하게, 건조된 펩티드를 재구성하기 위한 방법에서 단계 a)에서 출발 물질로 사용되는 바이얼 내의 건조된, 바람직하게는 동결건조된 펩타이드는 본 발명의 약학 조성물 내에 재구성되거나 및/또는 포함되는 펩타이드로서 상기 정의된 바와 같은 펩티드이다. 바람직하게, 상기 바이얼은 예방 및/또는 치료 방법, 바람직하게는 본원에서 정의된 바와 같은 치료 및/또는 예방 방법에서 단일 용량으로서의 주입량으로, 즉 단일 약학 투여 단위, 또는 실질적으로 동일한 시점에 대상자 신체의 다른 위치에 다중 주사의 경우 이의 일부로서 펩타이드를 포함한다. 대안적으로, 단계 a)에서 바이얼 내의 건조된 펩타이드의 양은 상기 방법에서 단일 용량으로서 주입하기 위한 양을 초과한다. 예를 들어, 바이얼 내의 펩타이드의 양은 단일 용량으로서 주입량의 두 배가 될 수 있다. 후자의 경우, 결국 방법 또는 치료 또는 예방시 주입을 위한 약학 조성물의 단일 용량이 되도록 재구성된 용량의 절반의 양은 본 발명의 약학 조성물과 같은 약학 조성물의 제조 방법에서 오일-기반 애주번트의 양과 혼합될 수 있으며, 또는, 택일적으로, 재구성된 용량의 총량은 결국 주입을 위한 약학 조성물의 2 용량이 되도록 오일-기반 애주번트의 양과 혼합될 수 있다.
바람직하게, 펩타이드를 재구성하는 방법의 단계 b)에서 펩타이드는 실온에서 약 5-30분, 또는 10-30분, 예를 들어 5, 10, 15, 20, 25 또는 30분 동안, 또는 그 사이의 임의의 수치의 시간 동안, 해동된다.
바람직하게, 펩타이드를 재구성하는 방법의 단계 d)에서의 혼합은 실온에서 바람직하게 약 0.5-2분 동안, 예를 들어 0.5, 1, 1.5 또는 2분 동안, 바이얼을 실질적으로 스월링하지 않고 이루어진다. 즉, 바람직하게 단계 d)의 펩타이드는 정지 상태에서 재구성 조성물과 혼합된다.
펩타이드를 재구성하는 방법의 단계 e)에서 스월링은 투명한 용액이 얻어질 때까지 스월링에 의해 수행된다. 언급된 바와 같이, 이는 바람직하게는 약 1-3분 동안 수행된다. 그러나, 일부 펩타이드에 대해서는 더 길거나 짧은 스월링 시간이 필요하다. 그러나, 투명한 용액은 바람직하게 20분 내에 얻을 수 있어야 한다. 따라서, 스월링은 1-20분, 1-10분, 1-5분 또는 1-3분, 예를 들어 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 15 또는 20분 또는 그 사이의 임의의 수치의 시간의 범위로, 바람직하게는 육안 검사시 투명 용액이 얻어질 때까지 수행될 수 있다.
펩타이드를 재구성하기 위한 방법의 단계 c)의 재구성 조성물 및 약학 조성물 제조 방법의 단계 (ii)의 오일-기반 애주번트는 본원에서 앞서 정의된 바와 같다. 바람직하게, 단계 c)에서의 재구성 조성물의 양은 약 0.5-2 mL의 범위, 바람직하게는 1 mL이다. 바람직하게, 단계 (i)에서 재구성된 펩타이드의 양은 단계 e) 후에 수득된, 즉 단계 e) 후 수득된 투명한 용액 내에 재구성된 펩타이드의 총량이다. 그러나, 상기 예시된 바와 같이, 선택적으로 덜 사용된다. 바람직하게, 이 재구성 조성물의 용량은 약 2:1, 1.9:1, 1.8:1, 1.7:1, 1.6:1, 1.5:1, 1.4:1, 1.1:1, 1:1, 1:1.9, 1:1.8, 1:1.7, 1:1.6, 1:1.5, 1:1.4, 1:1.3, 1:1.2, 또는 1:1.1, 바람직하게 1:1의 재구성 조성물:오일-기반 애주번트와 같이 약 2:1 내지 약 1:2의 비로 혼합된다.
(ii)에서의 커넥터는 이에 한정하는 것은 아니나, T 및 I 커넥터와 같은 2 개의 주사기 사이에 유체가 교환될 수 있게하는 2개의 주사기를 연결하는 당업계에 적합한 임의의 커넥터일 수 있다. 반복 (iv)은 이에 한정하는 것은 아니나, 10, 15, 20, 25, 30, 45, 50배 또는 그 사이의 임의의 값과 같은 약 10 내지 50회일 수있다.
부품 키트(Kit of parts)
또한,
1. 건조된, 바람직하게는 동결건조된 펩타이드를 함유하는 제1 바이얼로서, 여기서 상기 펩타이드는 바람직하게 본원에서 상기 정의된 바와 같은 펩티드인, 제1 바이얼;
2. 본 발명의 재구성 조성물을 함유하는 제2 바이얼; 및 선택적으로,
3. 오일-기반 애주번트, 바람직하게는 본원에서 상기 정의된 바와 같은, 오일-기반 애주번트를 함유하는 제3 바이얼
을 포함하는 부품 키트가 제공된다.
바람직하게, 모든 성분, 즉 건조된 펩타이드, 재구성 조성물 및 오일-기반 애주번트는 무균 및/또는 약학 등급 또는 임상 등급이다. 바람직하게, 이들 성분은 우수제조관리기준(Good manufacturing practice)(GMP)을 사용하여 제조되고, 유럽 의약청(European Medicines Agency) 및 식품 의약품 안전청(Food and Drug Administration)에 의해 정의된 바와 같은 GMP 품질을 갖는다.
바람직하게, 제1 바이얼은 재구성 조성물이 적어도 1개월, 2개월, 3개월, 6개월 또는 1년 또는 심지어 2년 동안 안정한 온도에서 저장된다. 바람직하게, 상기 온도는 -25℃ 내지 25℃, 또는 -23℃ 내지 -18℃, 또는 0℃ 내지 10℃, 또는 2℃ 내지 8℃, 또는 18℃ 내지 23℃이다. 바람직하게, 제2 바이얼은 재구성 조성물이 적어도 1개월, 2개월, 3개월, 6개월 또는 1년 또는 심지어 2년 동안 안정한 온도에서 저장된다. 바람직하게, 상기 온도는 -25℃ 내지 25℃, 또는 -23℃ 내지 -18℃, 또는 0℃ 내지 10℃, 또는 2℃ 내지 8℃, 또는 18℃ 내지 23℃이다. 바람직하게, 제3 바이얼은 재구성 조성물이 적어도 1개월, 2개월, 3개월, 6개월 또는 1년 또는 2년 동안 안정한 온도에서 저장된다. 바람직하게, 상기 온도는 -25℃ 내지 25℃, 또는 -23℃ 내지 -18℃, 또는 0℃ 내지 10℃, 또는 2℃ 내지 8℃, 또는 18℃ 내지 23℃이다. 바람직하게, 제1, 제2 및 제3 바이얼은 동일한 온도에서 저장된다.
선택적으로, 상기 부품 키트는 본원에서 상기 정의된 바와 같은 건조된 펩타이드를 재구성하는 방법, 보관 조건, 본원에서 상기 정의된 바와 같은 약학 조성물의 제조 방법이 기술된 매뉴얼 및/또는 제1, 제2 및/또는 제3 바이얼을 저장하 위한 매뉴얼을 추가로 포함한다. 또한, 상기 부품 키트는 제조될 약학 조성물을 투여하기 위한 매뉴얼을 포함할 수 있다. 바람직하게, 제1 바이얼, 제2 바이얼 및/또는 제3 바이얼의 용량은 최대 50 mL, 바람직하게는 0.1 내지 10 mL, 바람직하게는 1 내지 10 mL, 예를 들면, 0.5, 1, 2, 3, 4, 5 또는 10 mL, 또는 그 사이의 임의의 값이다. 바이얼은 본원에서 임의의 형상을 가질 수 있는 용기로서 이해되어야 한다. 선택적으로, 바이얼은 본 명세서에서 주사기로서 이해되어야 한다. 선택적으로, 제1 바이얼은 활성 처리 공정에 의해 커넥터를 통해 제2 바이얼에 연결되어 재구성 조성물이 펩타이드와 접촉 및 용해되도록 할 수 있다. 선택적으로, 제2 바이얼은 제3 바이얼에 연결되어 펩타이드를 포함하는 재구성 조성물이 오일-기반 애주번트와 혼합되도록 할 수 있다. 선택적으로, 부품 키트는 T- 커넥터와 같은 하나 이상의 커넥터 및/또는 바늘과 같은 주사 장치를 더 포함한다. 바람직하게, 제1 파일의 펩타이드의 양, 제2 파일의 재구성 조성물의 양 및/또는 제3 파일의 양 또는 오일-기반 애주번트의 양은 펩타이드를 재구성하는 방법 및/또는 본원에서 앞서 정의된 바와 같은 약학 조성물을 제조하는 방법에 정의된 바와 같다.
본 문헌 및 이의 청구범위에서 동사 "~을 구성하다(to comprise)" 및 이의 활용형은 비한정적인 의미로 사용되며, 상기 단어에 후속되는 아이템은 포함되지만 구체적으로 언급되지 않은 아이템은 제외되지 않는다. 또한, 부정관사 "하나의(a 또는 an)"에 의한 요소에 대한 언급은 문맥상 하나의 요소만이 명백하게 요구되는 경우를 제외하고는 하나 이상의 요소가 존재할 가능성을 배제하지 않는다. 따라서 부정관사 "하나의(a 또는 an)"는 일반적으로 "적어도 하나(at least one)"를 의미한다.
수치(예를 들어, 약 10)와 관련하여 사용될 경우 "약(about)" 또는 "대략(approximately)"이라는 단어는 바람직하게 수치가 수치의 0.1% 보다 많거나 적은 (10의) 주어진 수치일 수 있음을 의미한다.
본원에 제공된 서열 정보는 잘못 식별된 염기를 포함할 필요가 있는 것으로 좁게 해석되어서는 안된다. 숙련자는 이러한 잘못 식별된 염기를 식별할 수 있으며 이러한 오류를 수정하는 방법을 알고 있다.
본원에 인용된 모든 특허 및 문헌은 그 전체가 본원에 참고문헌으로 편입된다.
실시예
실시예 1
도입
본 연구의 목적은 펩타이드 Drug Product(약물 생성물) HPV-DP-6P 및 HPV-DP-7P의 용해, 및 이어서 Montanide ISA51VG를 이용한 에멀젼화를 포함한 다중 펩타이드 HPV 백신 생성물에 대한 적합한 재구성 방법을 찾는 것이었다. 이전의 연구들은 DMSO/WFI 제형에서 하나 이상의 시스테인 잔기를 함유하는 펩타이드가 디설파이드를 형성하는 경향이 강하다는 것을 보여주었다. Drug Product의 화학적 안정성을 향상시키고 펩타이드의 디설파이드 형성을 방지하기 위해 새로운 DMSO-프리 재구성 용액이 ㅁ모든 Drug Product의 재구성을 위해 개발되었다. 이 새로운 재구성 용액은 Drug Product를 용해시켜 Montanide ISA51VG와 안정한 에멀젼을 생성할 수 있어야한다. 디설파이드 형성은 최소화되어야 한다.
이 연구는 네 가지 수준의 분석으로 구성된다.
1. Drug Product를 재구성하고 육안 검사로 펩타이드의 용해를 모니터하기 위해 적합한 용매 조합을 스크리닝하는 단계.
2. Montanide를 이용한 Drug Product 에멀젼의 에멀션 안정성을 모니터하는 단계. 안정성은 육안 검사 및 에멀젼 드롭렛의 입자 크기의 분석을 통해 평가된다.
3. 레벨 1 및 2에서 성공적인 용매로 재구성한 후의 Drug Product의 화학적 안정성 분석.
4. 레벨 1, 2 및 3에서 성공적인 용매를 사용하여 재구성 및 에멀젼화한 후 Drug Product의 화학적 안정성 분석. 이 목적을 위해, 펩타이드를 Montanide ISA 51 VG로 용해, 에멀젼화화시킨 다음, 에멀젼으로부터의 추출 및 펩타이드 조성의 분석이 이루어진다.
재료
하기 동결건조된 펩타이드 조성물을 사용하였다: 바이얼 당 각 펩타이드 0.40 mg의 동일한 순량(바이얼 당 단백질의 총량은 2.00mg가 됨) 및 바이얼 당 0.56mg TFA로 혼합된 SEQ ID NO: 1-5으로 본원에서 표시된 펩타이드를 포함하는 DP-5P; 바이얼 당 각 펩타이드 0.40 mg의 동일한 순량(바이얼 당 단백질의 총량은 2.40mg가 됨) 및 바이얼 당 0.67mg TFA로 혼합된 SEQ ID NO: 1-6으로 본원에서 표시된 펩타이드를 포함하는 DP-6P; 및 바이얼 당 각 펩타이드 0.40 mg의 동일한 순량(바이얼 당 단백질의 총량은 2.80mg가 됨) 및 바이얼 당 0.96mg TFA로 혼합된 SEQ ID NO: 7-13으로 본원에서 표시된 펩타이드를 포함하는 DP-7P.
하기의 화학 물질을 사용하였다: Cremophor EL, (Sigma Aldrich, Kolliphor EL, C5135); Propylene Glycol 또는 PG(≥99.5%, Sigma Aldrich, W294004) 에탄올 또는 EtOH(Absolute, VWR Emprove® Ph Eur, BP, USP Article # 1.00986.1000); 시트르산 또는 CA(≥99%, Sigma Aldrich C1909); MilliQ 물(EQP-063에서); 무균 Montanide ISA 51VG(SEPPIC, batch# 14V011).
하기의 장비가 사용되었다: 주사기 압출 장치(Discofix-3 T-커넥터, B. Braun); DMSO-저항성 주사기(2mL NORM-JECT Luer Lock, Henke Sass Wolf); Waters UPLC/MS 시스템; Malvern Mastersizer 2000; Protein Simple MFI 5200 flowcell.
방법
용해
재구성 조성물은 동결건조된 Drug Product에 첨가하기 전에 유기 용매 및 수성 용매를 혼합하여 제조하였다. 1mL의 다양한 재구성 조성물을 Drug Product에 첨가하고, 용액을 여러 번 스월링하면서 혼합물을 5분간 방치하였다. 물리적 안정성은 육안 검사를 통해 평가하였다. 화학적 안정성은 UPLC/MS를 사용하여 평가하였다 (하기 Drug Product 용액의 화학적 안정성 참조).
Montanide를 이용한 에멀젼화
시각적으로 투명한 Drug Product 용액을 얻는 용제 조합은 Montanide ISA51 VG를 사용한 에멀젼화 실험에 사용되었다. 달리 명시되지 않는 한, 재구성 및 에멀젼화를 표 1의 프로토콜에 따라 수행하였다. 표시된 경우, 주사기 A 및 B의 내용물의 혼합을 다르게 수행하였다. 표 3의 절차에 대한 이러한 적응은 표 4 및 표 5의 결과 섹션에 나타내었다.
에멀젼 안정성 테스트를 위한 레이저 회절 실험
에멀젼 안정성은 육안 검사 및 Malvern Mastersizer 2000을 사용하여 입자 크기 분포 분석에 의해 모니터되었다.
입자 크기 분석을 위해, 에멀젼의 희석은 물로 또는 물에 용해된 0.01M 시트르산 용액으로 수행하여 원하는 수준의 차폐성(obscuration)을 얻었다. 1750 rpm의 속도에서 교반기를 사용하여 재구성된 DP를 포함하는 재구성 조성물과 Montanide를 혼합하고 1.46의 굴절률을 적용하였다. 입자 크기 분포는 용량-기반 분포에 대해 D(0.5)와 D(0.9)로 표현되었다.
에멀젼 안정성 테스트를 위한 마이크로 플로우 이미징(MFI)
에멀젼 안정성을 평가하기 위한 입자 크기 분석의 두 번째 기법으로, 마이크로 플로우 이미징(Micro Flow Imaging)이 사용되었다. 분석에 앞서, 에멀젼 1 드롭렛을 0.01M 수성 시트르산 용액 10mL에 첨가하고, 균질해질 때까지 혼합한 다음, 이 용액을 물에 1:100 희석하여 에멀젼의 희석물을 제조하였다. 샘플은 0.68분의 기간 동안 0.20mL의 퍼지 용량에서 또는 단일 실행으로 1백만 입자 당 측정되었다. 결과는 등가 원 직경(ECD)으로 표현된다.
Drug Product 용액의 화학적 안정성
완전한 용해 및 2시간 초과의 에멀젼 안정성을 나타내는 샘플의 경우, Waters Acquity 컬럼(타입: BEH130, C18, 1.7㎛, 2.1 x 150mm)을 사용하여 Waters TQD 질량 분석기에 연결된 Waters Acquity UPLC 시스템상의 UPLC/MS로 Drug Product 용액(추가 희석 없이)의 화학 안정성을 모니터하였다. 데이터 처리는 Masslynx 4.1 소프트웨어로 수행되었다. UV-검출을 220nm에서 수행하였고, 이동상은 0.3mL/분의 유속에서 물에 용해된 0.05% TFA 및 1% ACN(버퍼 A) 및 ACN에 용해된 0.05% TFA(버퍼 B)이었다. 컬럼 온도는 65℃이었고, 오토샘플러 온도는 5℃이었다. 5μL의 주입 용량을 사용하였고, 표 2의 구배 프로파일을 적용하였다.
구배의 전체 길이 동안 UV-검출을 수행하였고, 양성 모드에서 2-30분 동안 질량 분석을 수행하였다.
Drug Product 용액의 화학적 안정성을 분석하기 위해, 샘플을 용해 후 적어도 2시간까지 여러 시점에서 분석하였다.
HPV-DP-6P 및 HPV-DP-7P 백신 에멀젼의 사용중 화학적 안정성
완전한 용해, 2시간 초과의 에멀젼 안정성 및, 2시간 초과의 Drug Product 용액(추가 희석없이)의 화학적 안정성을 보여주는 샘플의 경우, Montanide ISA 51 VG를 사용한 백신 에멀젼의 사용중 화학 안정성을 UPLC/MS로 모니터하였다. 재구성되고 에멀젼화된 Drug Product의 화학적 안정성의 분석을 위해, 샘플을 용해 후 적어도 2시간까지 여러 시점에서 분석하였다. UPLC/MS 분석은 백신 에멀젼으로부터 펩타이드를 추출하기 위한 여분의 샘플 준비 단계를 사용하여, Drug Product 용액의 화학적 안정성에 대해 상술한 방법에 따라 수행하였다. 에멀젼화된 생성물의 샘플 준비를 위해, 하기의 단계가 적용되었다:
- 300μL 재구성 용액을 취하여 15mL Greiner 튜브에 첨가한다.
- 100μL 헵탄을 첨가한다.
- 200 μL의 Drug Product 에멀젼을 첨가한다. 용액을 위아래로 3회 피펫팅한다.
- 30초 동안 혼합물을 보텍싱한다.
- 4400rpm으로 5분간 원심분리하여 2상 시스템을 얻는다
- 20-200μL 피펫으로 바닥층에서 100μL 샘플을 취해 전체 회수 UPLC 바이얼에 옮긴다.
- Drug Product 용액의 화학적 안정성에 대해 기술된 방법에 따라 UPLC/UV/MS로 분석한다.
결과
재구성 및 에멀젼화를 위한 용매 스크리닝
동결건조된 펩타이드를 재구성하고 Montanide와 함께 화학적으로 및 물리적으로 안정한 에멀젼을 형성하기에 적합한 수성 및 유기 분획 모두를 포함하는 재구성 조성물을 정의하기 위해 용매를 스크리닝하였다. 아래의 모든 실험은 DP-6P를 사용하여 수행되었다. 실험은 DP-5P 및 DP-7P를 사용하여 검증되었지만, 데이터가 매우 대등하여, DP-6P의 데이터만 여기에 나타낸다. 이 스크린에서 재구성된 단백질 및 에멀젼의 물리적 안정성을 육안 검사로 평가하였다.
유기 분획으로서, 다양한 유기 용매가 시험되었다. WFI(주사용 수)와 혼합시 DP-6P를 완전히 용해시킬 수 있는 유일한 유기 용제는 NMP였다(표 3). 그러나, 재구성 조성물로서 NMP/WFI를 사용할 경우, Montanide를 갖는 안정한 에멀젼을 수득할 수 없었다. WFI 대신 식염수를 사용하면 에멀젼의 안정성이 약간 향상되었지만, 안정성이 2시간 이상인 에멀젼은 재현가능한 방식으로 얻을 수 없었다.
재구성시 유기 용매 혼합물
WFI와 조합하여 DP-6P가 완전히 용해된 단일 유기 용매는 확인되지 않았다. 따라서, 프로필렌 글리콜 및 다른 용매의 조합을 재구성 조성물 중의 유기 분획으로서 스크리닝하였다. 물리적 안정성은 육안 검사를 통해 평가되었다. 화학적 안정성은 UPLC/MS를 사용하여 평가하였다.
DP-6P의 완전한 용해는 여전히 관찰되지 않았지만, DP-6P의 용해에 대해 확인된 가장 선택적인 용매 조합은 에탄올, 프로필렌 글리콜 및 WFI가 함유된 에멀젼화제로서 Cremophor EL의 혼합물이었다(도 1).
디설파이드 형성을 제한하면서 용해 공정을 추가로 개선시키기 위해, 용매 혼합물(에탄올, 프로필렌 글리콜, Cremophor EL 및 WFI의 혼합물) 및 펩타이드 용액에 여러 항산화제 및 환원제를 첨가하는 효과를 평가하였다. 화학적 안정성을 UPLC/MS로 분석하여 디설파이드 형성의 정도를 모니터하였다. DTT(펩타이드에 비해 35몰 당량) 또는 아스코르브산(WFI 내의 0.1-1% 용액)의 첨가는 디설파이드 형성의 감소를 초래하지 않았지만, 용매 혼합물에 0.05-0.1M 수성 시트르산 용액의 첨가는 DP-6P의 용해를 개선시켰으며, 그리고 Drug Product의 용해 2시간 후 디설파이드 당 1% 이하의 면적% 값의 디설파이드 형성을 제한하였다. pH3 및 .05-0.1M의 농도에서 시트레이트 버퍼는 펩타이드 용해성이 낮기 때문에 에멀젼화에 사용할 수 없었다(데이터는 나타내지 않음). 도 2는 물, 프로필렌 글리콜 및 에탄올 중 1mg/mL 아스코르브산 대 물, 프로필렌 글리콜, 에탄올, 및 Cremophor EL 중 0.1M 시트르산의 혼합물에서 재구성된 DP의 시간(t=0 및 t=2h)에서의 화학적 안정성을 나타낸다.
재구성 후 및 후속 에멀젼화 후의 재구성 조성물의 시험
에멀젼화제로서 Cremophor EL은 보다 높은 투여량에서 보고된 부작용으로 인해 백신 제형에 덜 바람직하다. 그러나, Cremophor EL에 대한 대안으로 Tween 80, 시클로덱스트린 및 Triton X의 용해 및 에멀젼화 특성이 부적절하였다(데이터는 표시되지 않음). 육안 검사시, 프로필렌 글리콜, 에탄올, WFI 내의 시트르산 및 2% Tween 20의 조합을 사용하여 유망한 결과를 얻었다. 표 4에 요약된 바와 같은 에멀젼화 실험의 결과는 Cremophor EL 또는 Tween 20과 함께 프로필렌 글리콜 및 에탄올을 포함하는 에멀젼화제가 가장 안정한 에멀젼화제를 생성함을 보여준다. 그러나, DP-6P와 DP-7P 모두의 용액에서의 화학적 안정성은 Cremophor EL 대신에 Tween 20이 존재할 때, 현저히 나쁜 것으로, 즉, Drug Product의 용해 후 2시간에 디설파이드 당 5%가 넘는 면적% 값으로 나타났다(DP-6P의 UPLC 크로마토그램에 대해 도 3 참조; DP-5P 및 DP-7P의 결과는 매우 유사하였음(데이터는 표시되지 않음)).
표 4 및 도 3에 제시된 데이터를 종합하면, Cremophor EL은 생성물의 물리적 및 화학적 안정성 모두에 기초하여 Montanide가 함유된 DP-6P 에멀젼을 위한 에멀젼화로서 바람직하다는 결론을 내릴 수 있다.
용액에서의 Drug Product의 화학적 안정성에 대해 얻어진 결과가 백신 에멀젼에서의 Drug Product의 사용중 화학적 안정성으로 해석될 수 있음을 입증하기 위해, DP-6P 및 DP-7P 백신 에멀젼의 사용중 안정성을 조사하였으며, 그 결과는 도 4a, b, c 및 d에 제시되어 있다. 이 결과는 에멀젼화 단계 후에 백신 제조물의 Drug Product의 화학적 안정성이 유지된다는 것을 확인시켜 준다.
에멀젼화시 견고성을 위한 미세 조정
펩타이드 안정성 및 에멀젼 안정성
PG/EtOH/Cremophor EL의 비율을 변화시키고, 2가지 상이한 농도의 시트르산 용액을 시험하고, 상이한 유화 방법을 적용하고, 혼합물의 유기 대 수성 성분의 비율을 변화시킨 후속적인 일련의 실험을 수행하였다. 일반적으로, 1mL 재구성 조성물은 동결건조된 Drug Product에 첨가하기 전에 유기 용매 및 수성 용매를 혼합하여 제조하였다. 이어서, 표 5 및 6에 나타낸 바와 같이 상이한 혼합 단계 및/또는 커넥터를 사용하여 1mL의 수성 펩타이드 용액에 1mL의 Montanide를 첨가하여 에멀젼을 제조하였다.
보다 상세한 펩타이드 에멀션 안정성: 레이저 회절에 의한 PSD 분석
5개의 상이한 재구성 조성물에 대해, 입자 크기에 대한 상이한 에멀젼화 방법의 효과를 Malvern Mastersizer 2000을 사용하여 레이저 회절을 사용하여 분석 하였다. 모든 샘플에 대해, 유기 및 수성 용매를 동결건조된 Drug Product에 첨가하기 전에 혼합하여 제조하였다. 이어서, 수성 펩타이드 용액 1mL에 Montanide 1mL를 첨가하여 에멀젼을 제조하였다. 유기상과 수성상의 혼합은 3가지 상이한 방식으로 수행되었다:
- T-커넥터 프로세스를 사용하고 표 6에 표시된 혼합 사이클을 수행한다;
- I-커넥터를 사용하고 표 6에 표시된 혼합 사이클을 수행한다; 또는,
- 재구성 조성물에 펩타이드 용액을 함유하고 있는 바이얼에 Montanide 1mL를 첨가하고, 30초 동안 혼합물을 보텍싱한다.
결과의 요약을 표 6에 나타내었다. D(0.5)에 대한 근사값이 주어진다(용량 기반 분포).
표 5 및 표 6 모두에서, 상이한 혼합 방법 및/또는 사용된 상이한 타입의 커넥터 사이에 에멀젼 안정성의 차이가 관찰되지 않는 것으로 보인다. 그러나, 커넥터를 사용하는 대신에 혼합물을 보텍싱하면 입자 크기가 훨씬 큰 에멀젼이 발생되며, 이는 안정성이 덜 호의적이다. 일반적으로 입자 크기가 더 작은 에멀젼이 보다 안정하다.
또한, 에멀젼 안정성은 재구성 조성물의 총 용량에서 유기 분획(혼합물)의 퍼센트를 증가시킴으로써 개선되었다. 그러나, 여기서 시험된 가장 높은 용량의 유기 함량(300-400μL)은 Drug Product의 용해도를 감소시켰다. 그러므로, 유기 함량의 최적화는 재구성 조성물 mL 당 200 내지 300μL/mL(약 250μL)이었다. 또한, 시트르산(0.05 또는 0.1M) 용액의 농도 변화는 에멀젼 안정성에 영향을 미치지 않는 것으로 보이지만, 0.1M 시트르산 용액을 사용했을 경우에 약간 더 우수한 DP-6P의 용해가 얻어졌다.
마이크로 플로우 이미징을 이용한 입자 크기 분석
에멀젼의 에멀젼 안정성 및 입자 크기에 대한 시트르산 농도의 영향을 보다 상세하게 연구하기 위해, 추가의 입자 크기 분석 실험을 1mL의 Montanide로 에멀젼화한 후 최소 입자 크기를 생성하는 용매, 즉 1:3의 유기상 대 수성상 비율을 가지며, 여기서 유기상은 1:2:1의 PG 대 EtOH 대 Cremophor EL의 비율을 함유하는 용매를 사용하여 비교하였다(표 6). 수성상의 시트르산의 몰량을 변화시킨 직접 비교 실험을 수행하였다(0.05 및 0.1M 시트르산, 즉, 각각 0.038 및 0.075M 시트르산의 재구성 조성물 내에서의 시트르산의 최종 농도). DP-6P를 이러한 재구성 조성물 1mL에 용해시키고, 이어서 T-커넥터 공정을 사용하여 1mL의 Montanide로 에멀젼화시키고 50회의 패스트 혼합 사이클을 수행하였다. 이 실험에서, Drug Product 및 입자 크기의 모든 용해 및 에멀젼 안정성이 분석되었다. MFI 5200을 사용하여 판독 값으로 마이크로 플로우 이미징(MFI)을 수행하여 불규칙성을 시각적으로 조사할 수 있도록 카메라로 입자를 시각화하였다. 시트르산 재구성 조성물의 0.05 및 0.1M 시트르산의 PSD-비교를 도 5에 나타내었다.
도 5에서 볼 수 있듯이, 시트르산 용액의 농도는 에멀젼의 PSD에 영향을 미치지 않는다. 그러나, 0.1M 시트르산을 사용했을 때 Drug Product의 용해는 약간 더 우수하였다. 도 6은 DP-6P 에멀젼(도 6, 패널 a)의 3가지 독립적인 제조물 또는 제조후 2개의 상이한 시점에서 분석된 2가지 독립적인 제조물(도 6, 패널 b)의 MFI 결과를 나타내며, 여기서 Drug Product은 동일한 용매 조합(750μL 0.05M 시트르산 + 250μL PG/EtOH/Cremophor EL 1:2:1)을 사용하여 재구성되었다. 매우 견고한 PSD 결과가 얻어졌다. 또한, 에멀젼은 적어도 2시간 동안 모두 안정하였다.
DP-6P 및 DP-7P에 바람직한 재구성 용매 및 에멀젼화 방법의 적용
750μL 시트르산 용액 + 250μL PG/EtOH/Cremophor EL 1:2:1은 DP-6P 에멀젼에 대한 견고한 PSD 결과를 보여주었으며, 0.1M 시트르산을 사용하면 Drug Product의 가장 우수한 용해를 생성하였기 때문에, 이 용매 조합이 DP-6P 및 DP-7P 에멀젼의 제조를 위해 광범위하게 시험되었다.
DP-6P 및 DP-7P 에멀젼을 표 1의 지시에 따라 제조하였다. 간략히, 1mL의 재구성 조성물(750μL 0.1M 시트르산 + 250μL PG/EtOH/Cremophor EL 1:2:1을 동결건조된 Drug Product에 첨가하였으며, 그 결과 생성된 용액을 T-커넥터를 사용하여 50 패스트 혼합 사이클을 적용하여 1mL의 Montanide와 혼합하였다. MFI 분석을 위한 PSD 값은 ECD(등가 원 직경)로 주어지며 수에 기초한 분포가 주어진다. MFI 및 레이저 회절은 보완적인 기술이라는 점에 유의해야 한다. 따라서, 레이저 회절에 의해 그리고 MFI에 의해 얻어진 평균 입자 크기 값들의 직접적인 비교는 수행될 수 없다.
표 7 및 8은 750μL 0.1M 시트르산 + 250μL PG/EtOH/Cremophor EL 1:2:1을 포함하는 재구성 조성물(즉, 물에 용해된 750μL 0.1M 시트르산, 62.5μL 프로필렌 글리콜, 125μL 에탄올 및 62.5μL Cremophor EL)을 사용하여 적어도 3시간 동안 안정한 DP-6P 및 DP-7P 에멀젼 모두가 제조될 수 있음을 보여준다.
실시예 2
도입
CpG1826과 조합된 SLP 백신 접종의 치료 효능은 HPV16의 발암성 E6 및 E7 단백질을 발현하는 확립된 TC-1 종양을 갖는 마우스에서 이전에 입증되었다(Zwaveling et al., J. Immunol. (2002) 169:350-358). SLPs가 실시예 1에서 확인된 최적의 제형(750μL 0.1M 시트르산 + 250μL PG/EtOH/Cremophor EL 1:2:1)에서 기능을 보유하는지를 평가하기 위해, 본 발명자들은 DMSO/WFI 또는 신규한 재구성 조성물 중 어느 하나에서 재구성된 Db-제한 CTL 에피토프 RAHYNIVTF(본원에서 SEQ ID NO: 67로 나타냄)를 보유하는 SLP와 함께 TC-1 종양을 갖는 마우스를 치료적으로 백신 접종하였다. 모든 백신은 후속적으로 Montanide에서 에멀젼화되었다. 종양 성장은 75일 동안 모니터되었다. 백신-유도된 T 세포 반응의 피크에서, RAHYNIVTF-특이 CD8+ T 세포의 퍼센트 및 표현형이 혈액에서 검출되었다. DMSO/WFI에서 재구성된 SLP 및 신규한 재구성 조성물은 TC-1 종양 회귀 유도에서 유사한 효능을 나타냈다. 새로운 용액에 재구성된 SLP로 백신 접종된 마우스는 혈액내 RAHYNIVTF-특이 CD8+ T 세포의 비율이 더 높았다.
재료
방법
백신 제조
다음과 같은 그룹의 마우스가 연구에 포함되었다:
그룹 1: (n=5) Montanide ISA VG51로 1:1 에멀젼화된 40%v/v DMSO/WFI
그룹 2: (n=5) Montanide ISA VG51로 1:1 에멀젼화된 재구성 조성물(물에 용해된 750μL 0.1M 시트르산, 62.5μL 프로필렌 글리콜, 125μL 에탄올 및 mL 당 62.5μL Cremophor EL)
그룹 3: (n=10) Montanide ISA VG51로 1:1 에멀젼화된 40%v/v DMSO/WFI에 용해된 SLP GQAEPDRAHYNIVTFCCKCDSTLRLCVQSTHVDIR 및 20μg CpG ODN1826/마우스
그룹 4: (n=10) ontanide ISA VG51로 1:1 에멀젼화된 재구성 조성물(물에 용해된 750μL 0.1M 시트르산, 62.5μL 프로필렌 글리콜, 125μL 에탄올 및 mL 당 62.5μL Cremophor EL)에 용해된 SLP GQAEPDRAHYNIVTFCCKCDSTLRLCVQSTHVDIR(SEQ ID NO: 6) 및 20μg CpG ODN1826/마우스
그룹 1의 마우스를 위해, 400μL DMSO 및 600μL WFI를 혼합하고, 이어서 스월링함으로써 용액을 제조하였다. 그 용액을 2mL Luer-Lock 주사기(주사기 A)에 넣었다. 또 다른 2mL Luer-Lock 주사기(주사기 B)에 1mL의 Montanide ISA VG51을 넣고, 그 후 두 개의 주사기를 T-커넥터에 연결하였다. 내용물을 광범위하게 앞뒤로 혼합하여 에멀젼을 생성하였다. 혼합 후, 주사기를 분리하고, 25G 주사 바늘을 에멀젼을 함유하는 주사기에 배치하였다. 마우스 당 100μL을 좌측 측면 피하에 주사하였다.
그룹 2를 위해 제조된 백신은 동일한 방식으로 제조되었으나, 다만 DMSO 및 WFI 대신에 재구성 조성물(물에 용해된 750μL 0.1M 시트르산 및 250μL PG/EtOH/Cremophor EL 1:2:1, 즉 0.075M 시트르산, 6.25%v/v 프로필렌 글리콜 CAS 번호 57-55-6, 12.5%v/v 에탄올 및 물에 용해된 6.25%v/v 폴리옥시에틸렌글리세롤트리리시놀리에이트 35 CAS 번호 61791-12-6)을 사용한 것만 달리하였다. 그룹 3을 위한 백신은 본원에서 SEQ ID NO: 6(GQAEPDRAHYNIVTFCCKCDSTLRLCVQSTHVDIR)로 나타낸 1.5mg SLP를 함유하는 바이얼의 내용물을 400μL DMSO에 먼저 용해시킴으로써 제조하였다. SLP는 Fmoc 고체상 펩타이드 합성(Fmoc Solid Phase Peptide Synthesis, A Practical Approach, W.C. Chan, P.D. White Eds, Oxford Univ. Press 2000)을 통해 생성되었다. 그런 다음, DMSO 중의 펩타이드에 520μL WFI 및 80μL CpG ODN1826(스톡 5mg/㎖)을 첨가하였다. 이 용액을 2mL Luer-Lock 주사기에 취한 후, Montanide ISA VG51로 에멀젼화하여 그룹 1과 동일한 백신 제조 프로토콜을 따랐다. 그룹 4를 위한 백신의 제조는 그룹 3에 대한 프로토콜과 동일하지만, 다만 1.5mg SLP SEQ ID NO: 6을 함유하는 바이얼의 내용물을 920μL 재구성 조성물에 용해시키고 80μL CpG ODN1826(스톡 5mg/ml)에 첨가한 첫번째 단계만 달리하였다.
치료 백신
HPV16의 발암성 E6 및 E7 단백질을 발현하는 TC-1 종양 세포를 400μg/ml 제네티신(geneticin)이 보충된 완전 IMDM 배지에서 배양하였다. 0일째에, TC-1 세포를 트립신을 사용하여 수거하고, PBS/0.1% BSA로 3회 세척하였다. 수거 직후, 100,000 TC-1 세포에 40마리의 암컷 C57BL/6 마우스의 우측 측면에 s.c. 백신 접종하였다. 8일째, 모든 마우스에 백신 제조 섹션에서 설명한대로 좌측 측면에 s.c. 백신 접종하였다. 모든 마우스의 종양 크기는 종양 투여 후 75일까지의 캘리퍼를 사용하여 일주일에 적어도 2회 모니터하였다. 이 연구는 도 7에 나타낸 바와 같이 수행되었다.
혈액 내 T 세포 반응 강도의 측정
백신 접종 후 9 일째에, 모든 마우스의 꼬리 정맥에서 혈액을 채취하였다. 혈액 샘플을 96-웰 배양 플래이트에 옮기고 1600rpm으로 5분 동안 원심분리하였다. 오렌지색이 관찰될 때까지 혈구세포 펠렛을 라이시스 버퍼에 현탁시켜 적혈구를 용해시켰다. 이어서, 세포를 FACS 버퍼에서 세척하고, 형광 항체, Db-RAHYNIVTF-APC 테트라머 및 위의 재료 섹션에서 언급한 7-AAD로 염색하였다. 얼음에서 30분 동안 배양한 후 세포를 세척하고 Leiden University Medical Center(류마티스학과)의 BD LSRII 플로우 사이토미터로 분석하였다.
결과
백신 접종된 그룹 간의 유사한 종양 성장
적어도 일주일에 두 번 종양 크기를 모니터함으로써 각 개별 마우스에 대한 성장 곡선을 만들 수 있었다. 도 8에, 상이한 그룹에 대해 종양의 성장을 도시하였다. 종양 퇴행은 SLP 6 및 CpG1826으로 백신 접종된 모든 마우스에서 관찰된다. DMSO/WFI와 Montanide 또는 재구성 조성물과 Montanide 중 하나만을 투여받은 컨트롤 그룹의 종양은 빠르게 성장한다. 자연적 변이 외에도, SLP-백신 접종 그룹들 모두 사이에 명확한 차이는 관찰되지 않았다. 백신 접종된 그룹들 간에 차임가 없음을 보여주는, 카플란-마이어(Kaplan-Meier) 생존 플롯에 대해서는 도 9a를 참조바란다.
백신-유도성 테트라머 양성 CD8
+
T 세포
도 9b는 유도된 Db-RAYNIVTF(테트라머) 양성 CD8+ T 세포의 퍼센트를 나타낸다. 그룹 4(Rec. 조성 + SLP)의 마우스는 특정 뮤린 CD8+ T 세포의 프라이밍에 있어서 재구성 조성물에 제형화된 SLP 및 CpG가 DMSO/WFI 및 Montanide의 에멀젼에서 제형화된 SLP 및 CpG보다 더 효과적임을 나타내는 테트라머-양성 CD8+ T 세포 반응의 증진을 나타낸다. 그룹당 평균 퍼센트 및 표준 편차는 표 9를 참조바란다.
유의한 차이가 언페어드 t-테스트를 사용하여 결정되었으며, 이는 그룹 3과 4 사이에 p=0.022의 p-값을 생성하였다.
KLRG1 및 CD62L의 발현은 SLP 6 백신 접종 후 호의적인 항종양 발현 프로파일을 나타낸다
Van Duikeren 등(J Immunol, 2012; 189(7): 3397-403)에 의한 연구는 효과적인 항종양 반응의 유도와 상관 관계가 있는 파라미터를 확인하기 위한 것이었다. 이러한 바이오마커를 확인함으로써, 종양 모델에서 예후 가치가 있는 종양이 없는 마우스에서 다른 백신 조성물을 시험할 수 있다. 저자들은 한편으로는 KLRG1의 발현과 CD62L 발현의 부재 사이의 상관 관계를 그리고 다른 한편으로는 효과적인 항종양 면역 반응 사이의 상관 관계를 발견하였다. 플로우 사이토메트리를 이용하여 백신 접종 후 9일째에 백신 접종된 마우스의 혈액에서 KLRG1- 및 CD62L-발현 Db-RAHYNIVTF+ CD8+ T 세포의 퍼센트를 검출하였다. RAHYNIVTF-특이 KLRG1+ CD62L- CD8+ T 세포의 퍼센트 차이는 그룹 3과 4 사이에서 관찰되지 않았다. RAHYNIVTF-특이 CD8+ T 세포는 비히클만을 백신 접종한 마우스 그룹(그룹 1과 2)에서 KLRG1과 CD62L의 발현을 신뢰성있게 연구하기에는 충분히 검출되지 않았다. 그룹당 평균 퍼센트 및 표준 편차는 표 10을 참조바란다.
디스커션
DMSO/WFI 또는 재구성 조성물 중 어느 하나에 용해된 SLP 6으로 백신 접종된 마우스 그룹 사이에 전체 종양 성장에서 차이가 관찰되지 않았다. DMSO/WFI에 용해된 SLP로 백신 접종된 마우스 그룹과 비교하여 재구성 조성물에 용해된 SLP로 백신 접종된 마우스에서 특정 CD8+ T 세포의 유도가 증진된 것이 관찰되었다.
Montanide의 애주번팅 특성은 항원 디폿의 형성 및 항원 제시 세포의 성숙에 우호적인 국소 염증 및 세포 사멸의 유도로 인한 것이다. 재구성 조성물에 용해된 SLP로 백신 접종된 마우스 그룹에서 테트라머+ CD8+ T 세포의 증진된 유도는, 이 용액과 Montanide의 조합이 유익한 항원 방출 특성 또는 항원 제시 세포의 국소 자극을 갖는 에멀젼을 구성한다는 것을 제시한다. KLRG1 발현 및 CD62L의 부재의 우호적인 프로파일은 SLP를 사용한 두 그룹의 마우스 백신 접종 모두 간에 유사하였다. 상기 데이터는 본 발명의 재구성 조성물로 재구성된 SLPs가 본래 사용된 재구성 조성물(DMSO/WFI)과 비교하여 이들의 면역원성을 유지함을 입증한다.
실시예 3
재료
하기의 동결건조된 펩타이드 조성물을 사용하였다:
P53 DP5P: 본원에서 SEQ ID NO: 191, 193, 194, 201 및 203으로 나타낸 펩타이드를 포함함.
하기의 화학 물질을 사용하였다: Cremophor EL.(Sigma Aldrich, Kolliphor EL); 프로필렌 글리콜(≥99.5%, Sigma Aldrich); 에탄올(Absolute. VWR Emprove® Ph Eur.BP.USP); 시트르산(≥99%, Sigma Aldrich); MilliQ 물; 무균 Montanide ISA 51VG (SEPPIC.)
하기의 장비가 사용되었다: 주사기 압출 장치(Discofix-3 T-커넥터, B. Braun); DMSO-저항성 주사기(2mL NORM-JECT Luer Lock, Henke Sass Wolf); Waters UPLC/MS system EQP-004; Protein Simple MFI 5200
방법
백신 에멀젼 및 플라시보 에멀젼의 제조는 표 1에 기재된 바와 같이 수행하였다.
화학 안정성의 분석은 백신 에멀젼으로부터 펩타이드의 추출을 포함하여 HPV-DP-6P 및 HPV-DP-7P 백신 에멀젼의 사용중 화학 안정성의 분석 방법을 기술하는 섹션에서 실시예 1에 기술된 바와 같이 UPLC-MS에 의해 수행되었다.
입자 크기 분석은 Micro Flow Imaging에 의해 수행되었다. 분석에 앞서 10mL의 에멀젼을 10mL의 재구성 용액에 첨가하고 균질해질 때까지 혼합한 다음, 재구성 용액에 이 용액을 1:500으로 희석하여 백신 에멀젼의 희석물을 제조하였다.
MFI 5200의 분석 설정:
결과는 등가 원 직경(ECD)으로 표현되고, 수에 기초한 분포가 주어진다. 15μm 이상의 입자는 에멀젼 입자라기 보다는 인공물(artefacts)로 알려져 있기 때문에 결과에서 필터링된다.
결과
재구성된 약물 생성물(drug product)의 순도
상이한 시점에서의 Drug Product의 순도는 다음과 같이 계산되었다:
순도(%) = 100% - 불순물의 합계 ≥ 0.05% 면적
P53-DP-5P 백신 생성물의 사용 중 순도에 대한 오버뷰가 표 11에 주어진다.
표 11에서 볼 수 있듯이, Drug Products의 순도는 서서히 감소하지만 백신 제조 2시간 후에도 여전히 90.0% 이상이다. t=0 및 t=2h에서 백신의 UPLC 분석의 실시예 크로마토그램이 도 10에 제시된다.
면적이 1.0% 이상인 주요 피크와 불순물의 확인은 질량 분광기를 사용하여 수행되었다. 면적이 1.0% 이상인 모든 관련 물질은 측정 m/z 값을 펩타이드 서열의 분자량 및 이들의 공지되고 예상된 변형과 비교함으로써 보고되고 확인된다. 최대 3시간 동안 P53-DP-5P의 사용 중 저장에 대한 관련 물질의 결과 오버뷰가 표 12에 주어진다.
에멀젼으로부터 Drug Product의 회수
에멀젼으로부터 P53-DP-5P에 존재하는 5개의 개별 펩타이드의 회수는 에멀젼화 및 비-에멀젼화 샘플 신호의 비교에 의해 입증되었다. 결과의 오버뷰를 표 13에 나타내었다.
물리적 안정성
물리적 안정성은 MFI를 이용한 입자 크기 분석에 의해 분석되었다. 결과는 등가 원 직경(ECD)으로 표현된다. 평균 입자 크기 값은 수에 기반한 분포로부터 계산된 표 14에 주어진다.
결론
용해는 P53 항원(P53 DP-5P) 유래의 5 SLPs를 함유하는 혼합물에 대해 성공적으로 수행되었다.
백신 생성물의 화학적 및 물리적 사용중 안정성 모두를 조사하였다. P53 DP-5P에 대해 표 11에 요약된 관련 물질 분석 및 순도 계산은 백신 제조 2시간 후 Drug Product의 순도가 90.0% 이상임을 보여준다. 1%이상의 피크 면적%를 갖는 단지 하나의 관련 물질이 관찰되었다. MS-확인은 이 피크가 SEQ ID NO: 203에 제시된 펩타이드의 분자내 디설파이드임을 보여 주었다.
P53 DP-5P 백신 생성물의 물리적 안정성은 MFI로 입자 크기를 모니터함으로써 조사되었다. 입자 크기 분석의 결과는 표 14에 요약되어 있으며, 백신 제조 후 입자 크기가 최대 3시간까지 변하지 않음을 보여준다. 또한, 모든 백신 생성물은 안정성 연구 동안 육안 검사에 의해 모니터되었으며, 어떠한 시점에서도 상 분리가 관찰되지 않았다.
실시예 4
재료 및 방법
하기의 동결건조된 펩타이드 조성물이 사용되었다:
PRAME DP5P: SEQ ID NO: 153, 155, 156, 160 및 166으로 표시되는 펩타이드를 포함함.
5개의 PRAME 유래 펩타이드 세트는 UPLC 보유 시간, 아미노산 조성의 변화, 및 육안 검사에 의해 검출된 재구성 용액 중의 용해도에 기초하여 선택되었다.
사용된 다른 재료 및 방법은 실시예 3에서와 동일하다.
결과
재구성된 약물 생성물의 순도
상이한 시점에서의 약물 생성물의 순도는 다음과 같이 계산되었다:
순도(%) = 100% - 불순물의 합계 ≥0.05% 면적
PRAME-DP-5P 백신 생성물의 사용중 순도의 오버뷰를 표 15에 나타내었다. 동결건조된 PRAME-DP-5P의 순도는 이미 90% 미만임에 유의해야 한다. 그럼에도 불구하고, 시간 경과에 따른 순도의 매우 제한된 감소는 이 재구성된 약물 생성물의 양호한 화학적 안정성을 입증한다.
시간 경과에 따른 낮은 순도 감소는 높은 화학적 안정성을 나타낸다. PRAME-DP-5P에서 면적이 1.0% 이상인 불순물은 재구성 전 혼합물에 이미 존재하였다. 이 안정성 연구에서, 이러한 불순물의 유의한 증가가 관찰되지 않았으므로 불순물의 확인이 수행되지 않았다. 최대 3시간 동안 PRAME-DP-5P의 사용중 저장을 위한 관련 물질의 결과 오버뷰를 표 16에 나타내었다.
에멀젼으로부터 Drug Product의 회수
에멀젼으로부터 PRAME-DP-5P에 존재하는 5개의 개별 펩타이드의 회수는 에멀젼화 및 비-에멀젼화 샘플 신호의 비교에 의해 입증되었다. 결과에 대한 오버뷰를 표 17에 나타내었다.
결론
PRAME DP-5P의 순도는 완전히 만족스럽지 못했지만(<90%), 재구성된 백신 생성물의 순도 감소는 매우 제한적이었으며(순도 T=0 82.9%, T=3h 82.2%), 이는 본원에 기재된 조성물의 유익함을 확인시켜 주는 것이다.
SEQUENCE LISTING
<110> ISA Pharmaceuticals B.V.
<120> Formulation of a peptide vaccine
<130> P6060608PCT
<150> EP16175215.9
<151> 2016-06-20
<160> 232
<170> PatentIn version 3.3
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Ile Val Thr
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Asp Ile Arg
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Arg Lys Leu Pro Gln Leu Cys Thr Glu Leu Gln Thr Thr Ile His Asp
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<210> 13
<211> 32
<212> PRT
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<220>
<223> peptide
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Tyr Gly Thr Thr Leu Glu Gln Gln Tyr Asn Lys Pro Leu Cys Asp Leu
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Val Ser Leu Glu Val Tyr Leu Thr Ala Pro Thr Gly Cys Ile Lys Lys
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His Gly Tyr Thr Val Glu Val Gln Phe Asp Gly Asp Ile Cys Asn Thr
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Met His Tyr Thr Asn Trp Thr His Ile Tyr Ile Cys Glu Glu Ala Ser
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Val Thr Val Val Glu Gly Gln Val Asp Tyr Tyr Gly Leu Tyr Tyr Val
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His Glu Gly Ile Arg Thr Tyr Phe Val Gln Phe Lys Asp Asp Ala Glu
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Ile Leu Cys Pro Thr Ser Val Phe Ser Ser Asn Glu Val Ser Ser Pro
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Glu Ile Ile Arg Gln His Leu Ala Asn His Pro Ala Ala Thr His Thr
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Pro Arg Ser Glu Pro Asp Thr Gly Asn Pro Cys His Thr Thr Lys Leu
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Tyr Asp Ser Glu Trp Gln Arg Asp Gln Phe Leu Ser Gln Val Lys Ile
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<212> PRT
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Met His Gln Lys Arg Thr Ala Met Phe Gln Asp Pro Gln Glu Arg Pro
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Val Tyr Asp Phe Ala Phe Arg Asp Leu Cys Ile Val Tyr Arg Asp Gly
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Leu Arg Leu Cys Val Gln Ser Thr His Val Asp Ile Arg Thr Leu Glu
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Asp Leu Leu Met Gly Thr Leu Gly Ile Val Cys Pro Ile Cys Ser Gln
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Lys Pro
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Thr Asp Ala Gly Thr Trp Asp Lys Thr Ala Thr Cys Val Ser His Arg
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Gly Leu Tyr Tyr Val Lys Glu Gly Tyr Asn Thr Phe Tyr Ile Glu Phe
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Lys Ser Glu Cys Glu Lys Tyr Gly Asn Thr Gly Thr Trp Glu Val His
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Phe Gly Asn Asn Val Ile Asp Cys Asn Asp Ser Met Cys Ser Thr Ser
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Asp Asp Thr Val Ser Ala Thr Gln Leu Val Lys Gln Leu Gln His Thr
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<212> PRT
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Asn Pro Ala Glu Lys Leu Arg His Leu Asn Glu Lys Arg Arg Phe His
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<210> 19
<211> 105
<212> PRT
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Asp Asp Leu Arg Ala Phe Gln Gln Leu Phe Leu Asn Thr Leu Ser Phe
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Val Cys Pro Trp Cys Ala Ser Gln Gln
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<210> 20
<211> 30
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 20
Arg Pro Arg Lys Leu Pro Gln Leu Cys Thr Glu Leu Gln Thr Thr Ile
1 5 10 15
His Asp Ile Ile Leu Glu Cys Val Tyr Cys Lys Gln Gln Leu
20 25 30
<210> 21
<211> 22
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 21
Arg Arg Glu Val Tyr Asp Phe Ala Phe Arg Asp Leu Cys Ile Val Tyr
1 5 10 15
Arg Asp Gly Asn Pro Tyr
20
<210> 22
<211> 29
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 22
Ile Ser Glu Tyr Arg His Tyr Cys Tyr Ser Leu Tyr Gly Thr Thr Leu
1 5 10 15
Glu Gln Gln Tyr Asn Lys Pro Leu Cys Asp Leu Leu Ile
20 25
<210> 23
<211> 32
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 23
Ile Arg Cys Ile Asn Cys Gln Lys Pro Leu Cys Pro Glu Glu Lys Gln
1 5 10 15
Arg His Leu Asp Lys Lys Gln Arg Phe His Asn Ile Arg Gly Arg Trp
20 25 30
<210> 24
<211> 23
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 24
Gly Asp Thr Pro Thr Leu His Glu Tyr Met Leu Asp Leu Gln Pro Glu
1 5 10 15
Thr Thr Asp Leu Tyr Cys Tyr
20
<210> 25
<211> 17
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 25
Gln Ala Glu Pro Asp Arg Ala His Tyr Asn Ile Val Thr Phe Cys Cys
1 5 10 15
Lys
<210> 26
<211> 19
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 26
Leu Glu Asp Leu Leu Met Gly Thr Leu Gly Ile Val Cys Pro Ile Cys
1 5 10 15
Ser Gln Lys
<210> 27
<211> 8
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 27
Arg Pro Arg Lys Leu Pro Gln Leu
1 5
<210> 28
<211> 9
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 28
Lys Leu Pro Gln Leu Cys Thr Glu Leu
1 5
<210> 29
<211> 8
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 29
Leu Pro Gln Leu Cys Thr Glu Leu
1 5
<210> 30
<211> 10
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 30
Gln Leu Cys Thr Glu Leu Gln Thr Thr Ile
1 5 10
<210> 31
<211> 10
<212> PRT
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<223> peptide
<400> 31
Thr Glu Leu Gln Thr Thr Ile His Asp Ile
1 5 10
<210> 32
<211> 10
<212> PRT
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<223> peptide
<400> 32
Thr Ile His Asp Ile Ile Leu Arg Cys Val
1 5 10
<210> 33
<211> 9
<212> PRT
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<220>
<223> peptide
<400> 33
Ile Ile Leu Glu Cys Val Tyr Cys Lys
1 5
<210> 34
<211> 10
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 34
Leu Glu Cys Val Tyr Cys Lys Gln Gln Leu
1 5 10
<210> 35
<211> 8
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 35
Cys Val Tyr Cys Lys Gln Gln Leu
1 5
<210> 36
<211> 10
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 36
Arg Arg Glu Val Tyr Asp Phe Ala Phe Arg
1 5 10
<210> 37
<211> 9
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 37
Val Tyr Asp Phe Ala Phe Arg Asp Leu
1 5
<210> 38
<211> 8
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 38
Tyr Asp Phe Ala Phe Arg Asp Leu
1 5
<210> 39
<211> 9
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 39
Phe Ala Phe Arg Asp Leu Cys Ile Val
1 5
<210> 40
<211> 9
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 40
Phe Arg Asp Leu Cys Ile Val Tyr Arg
1 5
<210> 41
<211> 9
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 41
Ile Val Tyr Arg Asp Gly Asn Pro Tyr
1 5
<210> 42
<211> 9
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 42
Ile Ser Glu Tyr Arg His Tyr Cys Tyr
1 5
<210> 43
<211> 8
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 43
Ser Glu Tyr Arg His Tyr Cys Tyr
1 5
<210> 44
<211> 9
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 44
Cys Tyr Ser Leu Tyr Gly Thr Thr Leu
1 5
<210> 45
<211> 8
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 45
Thr Leu Glu Gln Gln Tyr Asn Lys
1 5
<210> 46
<211> 9
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 46
Leu Glu Gln Gln Tyr Asn Lys Pro Leu
1 5
<210> 47
<211> 8
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 47
Lys Pro Leu Cys Asp Leu Leu Ile
1 5
<210> 48
<211> 9
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 48
Cys Pro Glu Glu Lys Gln Arg His Leu
1 5
<210> 49
<211> 8
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 49
Pro Glu Glu Lys Gln Arg His Leu
1 5
<210> 50
<211> 7
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 50
Asp Lys Lys Gln Arg His Met
1 5
<210> 51
<211> 9
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 51
Lys Lys Gln Arg Phe His Asn Ile Arg
1 5
<210> 52
<211> 10
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 52
Gln Arg Phe His Asn Ile Arg Gly Arg Trp
1 5 10
<210> 53
<211> 9
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 53
Arg Phe His Asn Ile Arg Gly Arg Trp
1 5
<210> 54
<211> 9
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 54
Gly Asp Thr Pro Thr Leu His Glu Tyr
1 5
<210> 55
<211> 9
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 55
Thr Pro Thr Leu His Glu Tyr Met Leu
1 5
<210> 56
<211> 10
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 56
Tyr Met Leu Asp Leu Gln Pro Glu Thr Thr
1 5 10
<210> 57
<211> 9
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 57
Leu Gln Pro Glu Thr Thr Asp Leu Tyr
1 5
<210> 58
<211> 10
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 58
Gln Pro Glu Thr Thr Asp Leu Tyr Cys Tyr
1 5 10
<210> 59
<211> 9
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 59
Gln Ala Glu Pro Asp Arg Ala His Tyr
1 5
<210> 60
<211> 8
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 60
Ala Glu Pro Asp Arg Ala His Tyr
1 5
<210> 61
<211> 10
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 61
Glu Pro Asp Arg Ala His Tyr Asn Ile Val
1 5 10
<210> 62
<211> 7
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 62
Met Val Thr Phe Cys Cys Lys
1 5
<210> 63
<211> 9
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 63
Leu Glu Asp Leu Leu Met Gly Thr Leu
1 5
<210> 64
<211> 9
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 64
Leu Leu Met Gly Thr Leu Gly Ile Val
1 5
<210> 65
<211> 8
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 65
Thr Leu Gly Ile Val Cys Pro Ile
1 5
<210> 66
<211> 9
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 66
Ile Val Cys Pro Ile Cys Ser Gln Lys
1 5
<210> 67
<211> 9
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 67
Arg Ala His Tyr Asn Ile Val Thr Phe
1 5
<210> 68
<211> 90
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 68
Asp Tyr Trp Lys His Met Arg Leu Glu Cys Ala Ile Tyr Tyr Lys Ala
1 5 10 15
Arg Glu Met Gly Phe Lys His Ile Asn His Gln Val Val Pro Thr Leu
20 25 30
Ala Val Ser Lys Asn Lys Ala Leu Gln Ala Ile Glu Leu Gln Leu Thr
35 40 45
Leu Glu Thr Ile Tyr Asn Ser Gln Tyr Ser Asn Glu Lys Trp Thr Leu
50 55 60
Gln Asp Val Ser Leu Glu Val Tyr Leu Thr Ala Pro Thr Gly Cys Ile
65 70 75 80
Lys Lys His Gly Tyr Thr Val Glu Val Gln
85 90
<210> 69
<211> 45
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 69
Gln Val Asp Tyr Tyr Gly Leu Tyr Tyr Val His Glu Gly Ile Arg Thr
1 5 10 15
Tyr Phe Val Gln Phe Lys Asp Asp Ala Glu Lys Tyr Ser Lys Asn Lys
20 25 30
Val Trp Glu Val His Ala Gly Gly Gln Val Ile Leu Cys
35 40 45
<210> 70
<211> 95
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 70
Phe Asn Ser Ser His Lys Gly Arg Ile Asn Cys Asn Ser Asn Thr Thr
1 5 10 15
Pro Ile Val His Leu Lys Gly Asp Ala Asn Thr Leu Lys Cys Leu Arg
20 25 30
Tyr Arg Phe Lys Lys His Cys Thr Leu Tyr Thr Ala Val Ser Ser Thr
35 40 45
Trp His Trp Thr Gly His Asn Val Lys His Lys Ser Ala Ile Val Thr
50 55 60
Leu Thr Tyr Asp Ser Glu Trp Gln Arg Asp Gln Phe Leu Ser Gln Val
65 70 75 80
Lys Ile Pro Lys Thr Ile Thr Val Ser Thr Gly Phe Met Ser Ile
85 90 95
<210> 71
<211> 78
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 71
Ser Glu Tyr Arg His Tyr Cys Tyr Ser Leu Tyr Gly Thr Thr Leu Glu
1 5 10 15
Gln Gln Tyr Asn Lys Pro Leu Cys Asp Leu Leu Ile Arg Cys Ile Asn
20 25 30
Cys Gln Lys Pro Leu Cys Pro Glu Glu Lys Gln Arg His Leu Asp Lys
35 40 45
Lys Gln Arg Phe His Asn Ile Arg Gly Arg Trp Thr Gly Arg Cys Met
50 55 60
Ser Cys Cys Arg Ser Ser Arg Thr Arg Arg Glu Thr Gln Leu
65 70 75
<210> 72
<211> 47
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 72
Ser Ser Glu Glu Glu Asp Glu Ile Asp Gly Pro Ala Gly Gln Ala Glu
1 5 10 15
Pro Asp Arg Ala His Tyr Asn Ile Val Thr Phe Cys Cys Lys Cys Asp
20 25 30
Ser Thr Leu Arg Leu Cys Val Gln Ser Thr His Val Asp Ile Arg
35 40 45
<210> 73
<211> 15
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 73
Lys Ile Pro Lys Thr Ile Thr Val Ser Thr Gly Phe Met Ser Ile
1 5 10 15
<210> 74
<211> 15
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 74
Ser Ser Thr Trp His Trp Thr Gly His Asn Val Lys His Lys Ser
1 5 10 15
<210> 75
<211> 10
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 75
Phe Leu Ser Gln Val Lys Ile Pro Lys Thr
1 5 10
<210> 76
<211> 20
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 76
Phe Lys His Ile Asn His Gln Val Val Pro Thr Leu Ala Val Ser Lys
1 5 10 15
Asn Lys Ala Leu
20
<210> 77
<211> 16
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 77
Thr Leu Ala Val Ser Lys Asn Lys Ala Leu Gln Ala Ile Glu Leu Gln
1 5 10 15
<210> 78
<211> 15
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 78
Leu Tyr Thr Ala Val Ser Ser Thr Trp His Trp Thr Gly His Asn
1 5 10 15
<210> 79
<211> 13
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 79
Ala His Tyr Asn Ile Val Thr Phe Cys Cys Lys Cys Asp
1 5 10
<210> 80
<211> 35
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 80
Gly Gln Ala Glu Pro Asp Arg Ala His Tyr Asn Ile Val Thr Phe Cys
1 5 10 15
Cys Lys Cys Asp Ser Thr Leu Arg Leu Cys Val Gln Ser Thr His Val
20 25 30
Asp Ile Arg
35
<210> 81
<211> 16
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 81
Glu Asp Glu Ile Asp Gly Pro Ala Gly Gln Ala Glu Pro Asp Arg Ala
1 5 10 15
<210> 82
<211> 16
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 82
Asp Lys Lys Gln Arg Phe His Asn Ile Arg Gly Arg Trp Thr Gly Arg
1 5 10 15
<210> 83
<211> 22
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 83
Asp Pro Gln Glu Arg Pro Arg Lys Leu Pro Gln Leu Cys Thr Glu Leu
1 5 10 15
Gln Thr Thr Ile His Asp
20
<210> 84
<211> 32
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 84
Cys Val Tyr Cys Lys Gln Gln Leu Leu Arg Arg Glu Val Tyr Asp Phe
1 5 10 15
Ala Phe Arg Asp Leu Cys Ile Val Tyr Arg Asp Gly Asn Pro Tyr Ala
20 25 30
<210> 85
<211> 10
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 85
Phe Ala Phe Arg Asp Leu Cys Ile Val Tyr
1 5 10
<210> 86
<211> 32
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 86
Arg Asp Leu Cys Ile Val Tyr Arg Asp Gly Asn Pro Tyr Ala Val Cys
1 5 10 15
Asp Lys Cys Leu Lys Phe Tyr Ser Lys Ile Ser Glu Tyr Arg His Tyr
20 25 30
<210> 87
<211> 22
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 87
Tyr Arg Asp Gly Asn Pro Tyr Ala Val Cys Asp Lys Cys Leu Lys Phe
1 5 10 15
Tyr Ser Lys Ile Ser Glu
20
<210> 88
<211> 33
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 88
Cys Leu Lys Phe Tyr Ser Lys Ile Ser Glu Tyr Arg His Tyr Cys Tyr
1 5 10 15
Ser Leu Tyr Gly Thr Thr Leu Glu Gln Gln Tyr Asn Lys Pro Leu Cys
20 25 30
Asp
<210> 89
<211> 22
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 89
Tyr Gly Thr Thr Leu Glu Gln Gln Tyr Asn Lys Pro Leu Cys Asp Leu
1 5 10 15
Leu Ile Arg Cys Ile Asn
20
<210> 90
<211> 22
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 90
Lys Pro Leu Cys Asp Leu Leu Ile Arg Cys Ile Asn Cys Gln Lys Pro
1 5 10 15
Leu Cys Pro Glu Glu Lys
20
<210> 91
<211> 22
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 91
Glu Lys Gln Arg His Leu Asp Lys Lys Gln Arg Phe His Asn Ile Arg
1 5 10 15
Gly Arg Trp Thr Gly Arg
20
<210> 92
<211> 10
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 92
Lys Gln Arg Phe His Asn Ile Arg Gly Arg
1 5 10
<210> 93
<211> 22
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 93
Asp Leu Tyr Cys Tyr Glu Gln Leu Asn Asp Ser Ser Glu Glu Glu Asp
1 5 10 15
Glu Ile Asp Gly Pro Ala
20
<210> 94
<211> 22
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 94
His Tyr Asn Ile Val Thr Phe Cys Cys Lys Cys Asp Ser Thr Leu Arg
1 5 10 15
Leu Cys Val Gln Ser Thr
20
<210> 95
<211> 11
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 95
Ile Arg Thr Leu Glu Asp Leu Leu Met Gly Thr
1 5 10
<210> 96
<211> 22
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 96
Arg Glu His Gly Ile Gln Thr Leu Asn His Gln Val Val Pro Ala Tyr
1 5 10 15
Asn Ile Ser Lys Ser Lys
20
<210> 97
<211> 22
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 97
Asp Lys Cys Leu Lys Phe Tyr Ser Lys Ile Ser Glu Tyr Arg His Tyr
1 5 10 15
Cys Tyr Ser Leu Tyr Gly
20
<210> 98
<211> 32
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 98
Met His Gly Pro Lys Ala Thr Leu Gln Asp Ile Val Leu His Leu Glu
1 5 10 15
Pro Gln Asn Glu Ile Pro Val Asp Leu Leu Cys His Glu Gln Leu Ser
20 25 30
<210> 99
<211> 16
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 99
Ile Pro Val Asp Leu Leu Cys His Glu Gln Leu Ser Asp Ser Glu Glu
1 5 10 15
<210> 100
<211> 10
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 100
Gln Glu Arg Pro Arg Lys Leu Pro Gln Leu
1 5 10
<210> 101
<211> 10
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 101
Thr Ile His Asp Ile Ile Leu Glu Cys Val
1 5 10
<210> 102
<211> 10
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 102
Gly Arg Trp Thr Gly Arg Cys Met Ser Cys
1 5 10
<210> 103
<211> 10
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 103
Ser Ser Arg Thr Arg Arg Glu Thr Gln Leu
1 5 10
<210> 104
<211> 9
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 104
Ile Val Leu His Leu Glu Pro Gln Asn
1 5
<210> 105
<211> 845
<212> PRT
<213> Hepatitis B virus
<400> 105
Met Pro Leu Ser Tyr Gln His Phe Arg Lys Leu Leu Leu Leu Asp Asp
1 5 10 15
Gly Thr Glu Ala Gly Pro Leu Glu Glu Glu Leu Pro Arg Leu Ala Asp
20 25 30
Ala Asp Leu His Arg Arg Val Ala Glu Asp Leu Asn Leu Gly Asn Leu
35 40 45
Asn Val Ser Ile Pro Trp Thr His Lys Val Gly Asn Phe Thr Gly Leu
50 55 60
Tyr Ser Ser Thr Val Pro Ile Phe Asn Pro Glu Trp Gln Thr Pro Ser
65 70 75 80
Phe Pro Lys Ile His Leu Gln Glu Asp Ile Ile Asn Arg Cys Gln Gln
85 90 95
Phe Val Gly Pro Leu Thr Val Asn Glu Lys Arg Arg Leu Lys Leu Ile
100 105 110
Met Pro Ala Arg Phe Tyr Pro Thr His Thr Lys Tyr Leu Pro Leu Asp
115 120 125
Lys Gly Ile Lys Pro Tyr Tyr Pro Asp Gln Val Val Asn His Tyr Phe
130 135 140
Gln Thr Arg His Tyr Leu His Thr Leu Trp Lys Ala Gly Ile Leu Tyr
145 150 155 160
Lys Arg Glu Thr Thr Arg Ser Ala Ser Phe Cys Gly Ser Pro Tyr Ser
165 170 175
Trp Glu Gln Glu Leu Gln His Gly Arg Leu Val Ile Lys Thr Ser Gln
180 185 190
Arg His Gly Asp Glu Ser Phe Cys Ser Gln Ser Ser Gly Ile Leu Ser
195 200 205
Arg Ser Ser Val Gly Pro Cys Ile Arg Ser Gln Leu Lys Gln Ser Arg
210 215 220
Leu Gly Leu Gln Pro Arg Gln Gly Arg Leu Ala Ser Ser Gln Pro Ser
225 230 235 240
Arg Ser Gly Ser Ile Arg Ala Lys Ala His Pro Ser Thr Arg Arg Tyr
245 250 255
Phe Gly Val Glu Pro Ser Gly Ser Gly His Ile Asp His Ser Val Asn
260 265 270
Asn Ser Ser Ser Cys Leu His Gln Ser Ala Val Arg Lys Ala Ala Tyr
275 280 285
Ser His Leu Ser Thr Ser Lys Arg Gln Ser Ser Ser Gly His Ala Val
290 295 300
Glu Phe His Cys Leu Pro Pro Asn Ser Ala Gly Ser Gln Ser Gln Gly
305 310 315 320
Ser Val Ser Ser Cys Trp Trp Leu Gln Phe Arg Asn Ser Lys Pro Cys
325 330 335
Ser Glu Tyr Cys Leu Ser His Leu Val Asn Leu Arg Glu Asp Trp Gly
340 345 350
Pro Cys Asp Glu His Gly Glu His His Ile Arg Ile Pro Arg Thr Pro
355 360 365
Ala Arg Val Thr Gly Gly Val Phe Leu Val Asp Lys Asn Pro His Asn
370 375 380
Thr Ala Glu Ser Arg Leu Val Val Asp Phe Ser Gln Phe Ser Arg Gly
385 390 395 400
Ile Ser Arg Val Ser Trp Pro Lys Phe Ala Val Pro Asn Leu Gln Ser
405 410 415
Leu Thr Asn Leu Leu Ser Ser Asn Leu Ser Trp Leu Ser Leu Asp Val
420 425 430
Ser Ala Ala Phe Tyr His Ile Pro Leu His Pro Ala Ala Met Pro His
435 440 445
Leu Leu Ile Gly Ser Ser Gly Leu Ser Arg Tyr Val Ala Arg Leu Ser
450 455 460
Ser Asn Ser Arg Ile Asn Asn Asn Gln Tyr Gly Thr Met Gln Asn Leu
465 470 475 480
His Asp Ser Cys Ser Arg Gln Leu Tyr Val Ser Leu Met Leu Leu Tyr
485 490 495
Lys Thr Tyr Gly Trp Lys Leu His Leu Tyr Ser His Pro Ile Val Leu
500 505 510
Gly Phe Arg Lys Ile Pro Met Gly Val Gly Leu Ser Pro Phe Leu Leu
515 520 525
Ala Gln Phe Thr Ser Ala Ile Cys Ser Val Val Arg Arg Ala Phe Pro
530 535 540
His Cys Leu Ala Phe Ser Tyr Met Asp Asp Val Val Leu Gly Ala Lys
545 550 555 560
Ser Val Gln His Arg Glu Ser Leu Tyr Thr Ala Val Thr Asn Phe Leu
565 570 575
Leu Ser Leu Gly Ile His Leu Asn Pro Asn Lys Thr Lys Arg Trp Gly
580 585 590
Tyr Ser Leu Asn Phe Met Gly Tyr Ile Ile Gly Ser Trp Gly Thr Leu
595 600 605
Pro Gln Asp His Ile Val Gln Lys Ile Lys His Cys Phe Arg Lys Leu
610 615 620
Pro Val Asn Arg Pro Ile Asp Trp Lys Val Cys Gln Arg Ile Val Gly
625 630 635 640
Leu Leu Gly Phe Ala Ala Pro Phe Thr Gln Cys Gly Tyr Pro Ala Leu
645 650 655
Met Pro Leu Tyr Ala Cys Ile Gln Ala Lys Gln Ala Phe Thr Phe Ser
660 665 670
Pro Thr Tyr Lys Ala Phe Leu Ser Lys Gln Tyr Met Asn Leu Tyr Pro
675 680 685
Val Ala Arg Gln Arg Pro Gly Leu Cys Gln Val Phe Ala Asp Ala Thr
690 695 700
Pro Thr Gly Trp Gly Leu Ala Ile Gly His Gln Arg Met Arg Gly Thr
705 710 715 720
Phe Val Ala Pro Leu Pro Ile His Thr Ala Glu Leu Leu Ala Ala Cys
725 730 735
Phe Ala Arg Ser Arg Ser Gly Ala Lys Leu Ile Gly Thr Asp Asn Ser
740 745 750
Val Val Leu Ser Arg Lys Tyr Thr Ser Phe Pro Trp Leu Leu Gly Cys
755 760 765
Thr Ala Asn Trp Ile Leu Arg Gly Thr Ser Phe Val Tyr Val Pro Ser
770 775 780
Ala Leu Asn Pro Ala Asp Asp Pro Ser Arg Gly Arg Leu Gly Leu Ser
785 790 795 800
Arg Pro Leu Leu Arg Leu Pro Phe Gln Pro Thr Thr Gly Arg Thr Ser
805 810 815
Leu Tyr Ala Val Ser Pro Ser Val Pro Ser His Leu Pro Val Arg Val
820 825 830
His Phe Ala Ser Pro Leu His Val Ala Trp Arg Pro Pro
835 840 845
<210> 106
<211> 214
<212> PRT
<213> Hepatitis B virus
<400> 106
Met Gln Leu Phe His Leu Cys Leu Ile Ile Ser Cys Thr Cys Pro Thr
1 5 10 15
Val Gln Ala Ser Lys Leu Cys Leu Gly Trp Leu Trp Gly Met Asp Ile
20 25 30
Asp Pro Tyr Lys Glu Phe Gly Ala Thr Val Glu Leu Leu Ser Phe Leu
35 40 45
Pro Ser Asp Phe Phe Pro Ser Val Arg Asp Leu Leu Asp Thr Ala Ser
50 55 60
Ala Leu Tyr Arg Glu Ala Leu Glu Ser Pro Glu His Cys Ser Pro His
65 70 75 80
His Thr Ala Leu Arg Gln Ala Ile Leu Cys Trp Gly Glu Leu Met Thr
85 90 95
Leu Ala Thr Trp Val Gly Asn Asn Leu Glu Asp Pro Ala Ser Arg Asp
100 105 110
Leu Val Val Asn Tyr Val Asn Thr Asn Val Gly Leu Lys Ile Arg Gln
115 120 125
Leu Leu Trp Phe His Ile Ser Cys Leu Thr Phe Gly Arg Glu Thr Val
130 135 140
Leu Glu Tyr Leu Val Ser Phe Gly Val Trp Ile Arg Thr Pro Pro Ala
145 150 155 160
Tyr Arg Pro Pro Asn Ala Pro Ile Leu Ser Thr Leu Pro Glu Thr Thr
165 170 175
Val Val Arg Arg Arg Asp Arg Gly Arg Ser Pro Arg Arg Arg Thr Pro
180 185 190
Ser Pro Arg Arg Arg Arg Ser Pro Ser Pro Arg Arg Arg Arg Ser Gln
195 200 205
Ser Arg Glu Ser Gln Cys
210
<210> 107
<211> 154
<212> PRT
<213> Hepatitis B virus
<400> 107
Met Ala Ala Arg Leu Cys Cys Gln Leu Asp Pro Ala Arg Asp Val Leu
1 5 10 15
Cys Leu Arg Pro Val Gly Ala Glu Ser Arg Gly Arg Pro Leu Ser Gly
20 25 30
Pro Leu Gly Ala Leu Pro Ser Pro Ser Pro Ser Ala Val Pro Ala Asp
35 40 45
His Gly Ala His Leu Ser Leu Arg Gly Leu Pro Val Cys Ala Phe Ser
50 55 60
Ser Ala Gly Pro Cys Ala Leu Arg Phe Thr Ser Ala Arg Arg Met Glu
65 70 75 80
Thr Thr Val Asn Ala His Gln Ile Leu Pro Lys Val Leu His Lys Arg
85 90 95
Thr Leu Gly Leu Ser Ala Met Ser Thr Thr Asp Leu Glu Ala Tyr Phe
100 105 110
Lys Asp Cys Val Phe Lys Asp Trp Glu Glu Leu Gly Glu Glu Ile Arg
115 120 125
Leu Lys Val Phe Val Leu Gly Gly Cys Arg His Lys Leu Val Cys Ser
130 135 140
Pro Ala Pro Cys Asn Phe Phe Thr Ser Ala
145 150
<210> 108
<211> 400
<212> PRT
<213> Hepatitis B virus
<400> 108
Met Gly Gly Trp Ser Ser Lys Pro Arg Lys Gly Met Gly Thr Asn Leu
1 5 10 15
Ser Val Pro Asn Pro Leu Gly Phe Phe Pro Asp His Gln Leu Asp Pro
20 25 30
Ala Phe Gly Ala Asn Ser Asn Asn Pro Asp Trp Asp Phe Asn Pro Val
35 40 45
Lys Asp Asp Trp Pro Ala Ala Asn Gln Val Gly Val Gly Ala Phe Gly
50 55 60
Pro Arg Leu Thr Pro Pro His Gly Gly Ile Leu Gly Trp Ser Pro Gln
65 70 75 80
Ala Gln Gly Ile Leu Thr Thr Val Ser Thr Ile Pro Pro Pro Ala Ser
85 90 95
Thr Asn Arg Gln Ser Gly Arg Gln Pro Thr Pro Ile Ser Pro Pro Leu
100 105 110
Arg Asp Ser His Pro Gln Ala Met Gln Trp Asn Ser Thr Ala Phe His
115 120 125
Gln Thr Leu Gln Asp Pro Arg Val Arg Gly Leu Tyr Leu Pro Ala Gly
130 135 140
Gly Ser Ser Ser Gly Thr Val Asn Pro Ala Pro Asn Ile Ala Ser His
145 150 155 160
Ile Ser Ser Ile Ser Ala Arg Thr Gly Asp Pro Val Thr Asn Met Glu
165 170 175
Asn Ile Thr Ser Gly Phe Leu Gly Pro Leu Leu Val Leu Gln Ala Gly
180 185 190
Phe Phe Leu Leu Thr Arg Ile Leu Thr Ile Pro Gln Ser Leu Asp Ser
195 200 205
Trp Trp Thr Ser Leu Asn Phe Leu Gly Gly Ser Pro Val Cys Leu Gly
210 215 220
Gln Asn Ser Gln Ser Pro Thr Ser Asn His Ser Pro Thr Ser Cys Pro
225 230 235 240
Pro Ile Cys Pro Gly Tyr Arg Trp Met Cys Leu Arg Arg Phe Ile Ile
245 250 255
Phe Leu Phe Ile Leu Leu Leu Cys Leu Ile Phe Leu Leu Val Leu Leu
260 265 270
Asp Tyr Gln Gly Met Leu Pro Val Cys Pro Leu Ile Pro Gly Ser Thr
275 280 285
Thr Thr Ser Thr Gly Pro Cys Lys Thr Cys Thr Thr Pro Ala Gln Gly
290 295 300
Asn Ser Met Phe Pro Ser Cys Cys Cys Thr Lys Pro Thr Asp Gly Asn
305 310 315 320
Cys Thr Cys Ile Pro Ile Pro Ser Ser Trp Ala Phe Ala Lys Tyr Leu
325 330 335
Trp Glu Trp Ala Ser Val Arg Phe Ser Trp Leu Ser Leu Leu Val Pro
340 345 350
Phe Val Gln Trp Phe Val Gly Leu Ser Pro Thr Val Trp Leu Ser Ala
355 360 365
Ile Trp Met Met Trp Tyr Trp Gly Pro Ser Leu Tyr Ser Ile Val Ser
370 375 380
Pro Phe Ile Pro Leu Leu Pro Ile Phe Phe Cys Leu Trp Val Tyr Ile
385 390 395 400
<210> 109
<211> 30
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 109
Met Pro Leu Ser Tyr Gln His Phe Arg Lys Leu Leu Leu Leu Asp Asp
1 5 10 15
Gly Thr Glu Ala Gly Pro Leu Glu Glu Glu Leu Pro Arg Leu
20 25 30
<210> 110
<211> 35
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 110
Ile Pro Trp Thr His Lys Val Gly Asn Phe Thr Gly Leu Tyr Ser Ser
1 5 10 15
Thr Val Pro Ile Phe Asn Pro Glu Trp Gln Thr Pro Ser Phe Pro Lys
20 25 30
Ile His Leu
35
<210> 111
<211> 33
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 111
Val Asn Glu Lys Arg Arg Leu Lys Leu Ile Met Pro Ala Arg Phe Tyr
1 5 10 15
Pro Thr His Thr Lys Tyr Leu Pro Leu Asp Lys Gly Ile Lys Pro Tyr
20 25 30
Tyr
<210> 112
<211> 33
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 112
Tyr Pro Thr His Thr Lys Tyr Leu Pro Leu Asp Lys Gly Ile Lys Pro
1 5 10 15
Tyr Tyr Pro Asp Gln Val Val Asn His Tyr Phe Gln Thr Arg His Tyr
20 25 30
Leu
<210> 113
<211> 39
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 113
Val Val Asn His Tyr Phe Gln Thr Arg His Tyr Leu His Thr Leu Trp
1 5 10 15
Lys Ala Gly Ile Leu Tyr Lys Arg Glu Thr Thr Arg Ser Ala Ser Phe
20 25 30
Cys Gly Ser Pro Tyr Ser Trp
35
<210> 114
<211> 35
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 114
Tyr Phe Gln Thr Arg His Tyr Leu His Thr Leu Trp Lys Ala Gly Ile
1 5 10 15
Leu Tyr Lys Arg Glu Thr Thr Arg Ser Ala Ser Phe Cys Gly Ser Pro
20 25 30
Tyr Ser Trp
35
<210> 115
<211> 34
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 115
Asp Gln Val Val Asn His Tyr Phe Gln Thr Arg His Tyr Leu His Thr
1 5 10 15
Leu Trp Lys Ala Gly Ile Leu Tyr Lys Arg Glu Thr Thr Arg Ser Ala
20 25 30
Ser Phe
<210> 116
<211> 32
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 116
Ser Gln Ser Gln Gly Ser Val Ser Ser Cys Trp Trp Leu Gln Phe Arg
1 5 10 15
Asn Ser Lys Pro Cys Ser Glu Tyr Cys Leu Ser His Leu Val Asn Leu
20 25 30
<210> 117
<211> 33
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 117
Thr Ala Glu Ser Arg Leu Val Val Asp Phe Ser Gln Phe Ser Arg Gly
1 5 10 15
Ile Ser Arg Val Ser Trp Pro Lys Phe Ala Val Pro Asn Leu Gln Ser
20 25 30
Leu
<210> 118
<211> 38
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 118
Asn Leu Leu Ser Ser Asn Leu Ser Trp Leu Ser Leu Asp Val Ser Ala
1 5 10 15
Ala Phe Tyr His Ile Pro Leu His Pro Ala Ala Met Pro His Leu Leu
20 25 30
Ile Gly Ser Ser Gly Leu
35
<210> 119
<211> 38
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 119
Ser Ser Asn Leu Ser Trp Leu Ser Leu Asp Val Ser Ala Ala Phe Tyr
1 5 10 15
His Ile Pro Leu His Pro Ala Ala Met Pro His Leu Leu Ile Gly Ser
20 25 30
Ser Gly Leu Ser Arg Tyr
35
<210> 120
<211> 33
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 120
Trp Leu Ser Leu Asp Val Ser Ala Ala Phe Tyr His Ile Pro Leu His
1 5 10 15
Pro Ala Ala Met Pro His Leu Leu Ile Gly Ser Ser Gly Leu Ser Arg
20 25 30
Tyr
<210> 121
<211> 34
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 121
His Asp Ser Cys Ser Arg Gln Leu Tyr Val Ser Leu Met Leu Leu Tyr
1 5 10 15
Lys Thr Tyr Gly Trp Lys Leu His Leu Tyr Ser His Pro Ile Val Leu
20 25 30
Gly Phe
<210> 122
<211> 36
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 122
Ser Pro Phe Leu Leu Ala Gln Phe Thr Ser Ala Ile Cys Ser Val Val
1 5 10 15
Arg Arg Ala Phe Pro His Cys Leu Ala Phe Ser Tyr Met Asp Asp Val
20 25 30
Val Leu Gly Ala
35
<210> 123
<211> 34
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 123
Phe Leu Leu Ala Gln Phe Thr Ser Ala Ile Cys Ser Val Val Arg Arg
1 5 10 15
Ala Phe Pro His Cys Leu Ala Phe Ser Tyr Met Asp Asp Val Val Leu
20 25 30
Gly Ala
<210> 124
<211> 34
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 124
Arg Glu Ser Leu Tyr Thr Ala Val Thr Asn Phe Leu Leu Ser Leu Gly
1 5 10 15
Ile His Leu Asn Pro Asn Lys Thr Lys Arg Trp Gly Tyr Ser Leu Asn
20 25 30
Phe Met
<210> 125
<211> 34
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 125
Asn Pro Asn Lys Thr Lys Arg Trp Gly Tyr Ser Leu Asn Phe Met Gly
1 5 10 15
Tyr Ile Ile Gly Ser Trp Gly Thr Leu Pro Gln Asp His Ile Val Gln
20 25 30
Lys Ile
<210> 126
<211> 39
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 126
Tyr Pro Ala Leu Met Pro Leu Tyr Ala Cys Ile Gln Ala Lys Gln Ala
1 5 10 15
Phe Thr Phe Ser Pro Thr Tyr Lys Ala Phe Leu Ser Lys Gln Tyr Met
20 25 30
Asn Leu Tyr Pro Val Ala Arg
35
<210> 127
<211> 35
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 127
Met Pro Leu Tyr Ala Cys Ile Gln Ala Lys Gln Ala Phe Thr Phe Ser
1 5 10 15
Pro Thr Tyr Lys Ala Phe Leu Ser Lys Gln Tyr Met Asn Leu Tyr Pro
20 25 30
Val Ala Arg
35
<210> 128
<211> 32
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 128
Gln Arg Met Arg Gly Thr Phe Val Ala Pro Leu Pro Ile His Thr Ala
1 5 10 15
Glu Leu Leu Ala Ala Cys Phe Ala Arg Ser Arg Ser Gly Ala Lys Leu
20 25 30
<210> 129
<211> 38
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 129
Val Leu Ser Arg Lys Tyr Thr Ser Phe Pro Trp Leu Leu Gly Cys Thr
1 5 10 15
Ala Asn Trp Ile Leu Arg Gly Thr Ser Phe Val Tyr Val Pro Ser Ala
20 25 30
Leu Asn Pro Ala Asp Asp
35
<210> 130
<211> 36
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 130
Arg Lys Tyr Thr Ser Phe Pro Trp Leu Leu Gly Cys Thr Ala Asn Trp
1 5 10 15
Ile Leu Arg Gly Thr Ser Phe Val Tyr Val Pro Ser Ala Leu Asn Pro
20 25 30
Ala Asp Asp Pro
35
<210> 131
<211> 36
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 131
Val Leu Ser Arg Lys Tyr Thr Ser Phe Pro Trp Leu Leu Gly Cys Thr
1 5 10 15
Ala Asn Trp Ile Leu Arg Gly Thr Ser Phe Val Tyr Val Pro Ser Ala
20 25 30
Leu Asn Pro Ala
35
<210> 132
<211> 35
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 132
Asp Pro Ala Ser Arg Asp Leu Val Val Asn Tyr Val Asn Thr Asn Val
1 5 10 15
Gly Leu Lys Ile Arg Gln Leu Leu Trp Phe His Ile Ser Cys Leu Thr
20 25 30
Phe Gly Arg
35
<210> 133
<211> 34
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 133
Cys Leu Thr Phe Gly Arg Glu Thr Val Leu Glu Tyr Leu Val Ser Phe
1 5 10 15
Gly Val Trp Ile Arg Thr Pro Pro Ala Tyr Arg Pro Pro Asn Ala Pro
20 25 30
Ile Leu
<210> 134
<211> 33
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 134
Ala Leu Pro Ser Pro Ser Pro Ser Ala Val Pro Ala Asp His Gly Ala
1 5 10 15
His Leu Ser Leu Arg Gly Leu Pro Val Cys Ala Phe Ser Ser Ala Gly
20 25 30
Pro
<210> 135
<211> 35
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 135
Cys Ala Phe Ser Ser Ala Gly Pro Cys Ala Leu Arg Phe Thr Ser Ala
1 5 10 15
Arg Arg Met Glu Thr Thr Val Asn Ala His Gln Ile Leu Pro Lys Val
20 25 30
Leu His Lys
35
<210> 136
<211> 35
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 136
His Gln Ile Leu Pro Lys Val Leu His Lys Arg Thr Leu Gly Leu Ser
1 5 10 15
Ala Met Ser Thr Thr Asp Leu Glu Ala Tyr Phe Lys Asp Cys Val Phe
20 25 30
Lys Asp Trp
35
<210> 137
<211> 34
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 137
Leu Glu Ala Tyr Phe Lys Asp Cys Val Phe Lys Asp Trp Glu Glu Leu
1 5 10 15
Gly Glu Glu Ile Arg Leu Lys Val Phe Val Leu Gly Gly Cys Arg His
20 25 30
Lys Leu
<210> 138
<211> 36
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 138
Met Glu Asn Ile Thr Ser Gly Phe Leu Gly Pro Leu Leu Val Leu Gln
1 5 10 15
Ala Gly Phe Phe Leu Leu Thr Arg Ile Leu Thr Ile Pro Gln Ser Leu
20 25 30
Asp Ser Trp Trp
35
<210> 139
<211> 36
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 139
Cys Pro Pro Ile Cys Pro Gly Tyr Arg Trp Met Cys Leu Arg Arg Phe
1 5 10 15
Ile Ile Phe Leu Phe Ile Leu Leu Leu Cys Leu Ile Phe Leu Leu Val
20 25 30
Leu Leu Asp Tyr
35
<210> 140
<211> 36
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 140
Cys Ile Pro Ile Pro Ser Ser Trp Ala Phe Ala Lys Tyr Leu Trp Glu
1 5 10 15
Trp Ala Ser Val Arg Phe Ser Trp Leu Ser Leu Leu Val Pro Phe Val
20 25 30
Gln Trp Phe Val
35
<210> 141
<211> 32
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 141
Pro Ser Ser Trp Ala Phe Ala Lys Tyr Leu Trp Glu Trp Ala Ser Val
1 5 10 15
Arg Phe Ser Trp Leu Ser Leu Leu Val Pro Phe Val Gln Trp Phe Val
20 25 30
<210> 142
<211> 31
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 142
Ser Ser Trp Ala Phe Ala Lys Tyr Leu Trp Glu Trp Ala Ser Val Arg
1 5 10 15
Phe Ser Trp Leu Ser Leu Leu Val Pro Phe Val Gln Trp Phe Val
20 25 30
<210> 143
<211> 36
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 143
Trp Leu Ser Ala Ile Trp Met Met Trp Tyr Trp Gly Pro Ser Leu Tyr
1 5 10 15
Ser Ile Val Ser Pro Phe Ile Pro Leu Leu Pro Ile Phe Phe Cys Leu
20 25 30
Trp Val Tyr Ile
35
<210> 144
<211> 30
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 144
Met Met Trp Tyr Trp Gly Pro Ser Leu Tyr Ser Ile Val Ser Pro Phe
1 5 10 15
Ile Pro Leu Leu Pro Ile Phe Phe Cys Leu Trp Val Tyr Ile
20 25 30
<210> 145
<211> 31
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 145
Trp Met Met Trp Tyr Trp Gly Pro Ser Leu Tyr Ser Ile Val Ser Pro
1 5 10 15
Phe Ile Pro Leu Leu Pro Ile Phe Phe Cys Leu Trp Val Tyr Ile
20 25 30
<210> 146
<211> 37
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 146
Met Gln Leu Phe His Leu Cys Leu Ile Ile Ser Cys Thr Cys Pro Thr
1 5 10 15
Val Gln Ala Ser Lys Leu Cys Leu Gly Trp Leu Trp Gly Met Asp Ile
20 25 30
Asp Pro Tyr Lys Glu
35
<210> 147
<211> 509
<212> PRT
<213> Homo sapiens
<400> 147
Met Glu Arg Arg Arg Leu Trp Gly Ser Ile Gln Ser Arg Tyr Ile Ser
1 5 10 15
Met Ser Val Trp Thr Ser Pro Arg Arg Leu Val Glu Leu Ala Gly Gln
20 25 30
Ser Leu Leu Lys Asp Glu Ala Leu Ala Ile Ala Ala Leu Glu Leu Leu
35 40 45
Pro Arg Glu Leu Phe Pro Pro Leu Phe Met Ala Ala Phe Asp Gly Arg
50 55 60
His Ser Gln Thr Leu Lys Ala Met Val Gln Ala Trp Pro Phe Thr Cys
65 70 75 80
Leu Pro Leu Gly Val Leu Met Lys Gly Gln His Leu His Leu Glu Thr
85 90 95
Phe Lys Ala Val Leu Asp Gly Leu Asp Val Leu Leu Ala Gln Glu Val
100 105 110
Arg Pro Arg Arg Trp Lys Leu Gln Val Leu Asp Leu Arg Lys Asn Ser
115 120 125
His Gln Asp Phe Trp Thr Val Trp Ser Gly Asn Arg Ala Ser Leu Tyr
130 135 140
Ser Phe Pro Glu Pro Glu Ala Ala Gln Pro Met Thr Lys Lys Arg Lys
145 150 155 160
Val Asp Gly Leu Ser Thr Glu Ala Glu Gln Pro Phe Ile Pro Val Glu
165 170 175
Val Leu Val Asp Leu Phe Leu Lys Glu Gly Ala Cys Asp Glu Leu Phe
180 185 190
Ser Tyr Leu Ile Glu Lys Val Lys Arg Lys Lys Asn Val Leu Arg Leu
195 200 205
Cys Cys Lys Lys Leu Lys Ile Phe Ala Met Pro Met Gln Asp Ile Lys
210 215 220
Met Ile Leu Lys Met Val Gln Leu Asp Ser Ile Glu Asp Leu Glu Val
225 230 235 240
Thr Cys Thr Trp Lys Leu Pro Thr Leu Ala Lys Phe Ser Pro Tyr Leu
245 250 255
Gly Gln Met Ile Asn Leu Arg Arg Leu Leu Leu Ser His Ile His Ala
260 265 270
Ser Ser Tyr Ile Ser Pro Glu Lys Glu Glu Gln Tyr Ile Ala Gln Phe
275 280 285
Thr Ser Gln Phe Leu Ser Leu Gln Cys Leu Gln Ala Leu Tyr Val Asp
290 295 300
Ser Leu Phe Phe Leu Arg Gly Arg Leu Asp Gln Leu Leu Arg His Val
305 310 315 320
Met Asn Pro Leu Glu Thr Leu Ser Ile Thr Asn Cys Arg Leu Ser Glu
325 330 335
Gly Asp Val Met His Leu Ser Gln Ser Pro Ser Val Ser Gln Leu Ser
340 345 350
Val Leu Ser Leu Ser Gly Val Met Leu Thr Asp Val Ser Pro Glu Pro
355 360 365
Leu Gln Ala Leu Leu Glu Arg Ala Ser Ala Thr Leu Gln Asp Leu Val
370 375 380
Phe Asp Glu Cys Gly Ile Thr Asp Asp Gln Leu Leu Ala Leu Leu Pro
385 390 395 400
Ser Leu Ser His Cys Ser Gln Leu Thr Thr Leu Ser Phe Tyr Gly Asn
405 410 415
Ser Ile Ser Ile Ser Ala Leu Gln Ser Leu Leu Gln His Leu Ile Gly
420 425 430
Leu Ser Asn Leu Thr His Val Leu Tyr Pro Val Pro Leu Glu Ser Tyr
435 440 445
Glu Asp Ile His Gly Thr Leu His Leu Glu Arg Leu Ala Tyr Leu His
450 455 460
Ala Arg Leu Arg Glu Leu Leu Cys Glu Leu Gly Arg Pro Ser Met Val
465 470 475 480
Trp Leu Ser Ala Asn Pro Cys Pro His Cys Gly Asp Arg Thr Phe Tyr
485 490 495
Asp Pro Glu Pro Ile Leu Cys Pro Cys Phe Met Pro Asn
500 505
<210> 148
<211> 33
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 148
Met Glu Arg Arg Arg Leu Trp Gly Ser Ile Gln Ser Arg Tyr Ile Ser
1 5 10 15
Met Ser Val Trp Thr Ser Pro Arg Arg Leu Val Glu Leu Ala Gly Gln
20 25 30
Ser
<210> 149
<211> 35
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 149
Val Trp Thr Ser Pro Arg Arg Leu Val Glu Leu Ala Gly Gln Ser Leu
1 5 10 15
Leu Lys Asp Glu Ala Leu Ala Ile Ala Ala Leu Glu Leu Leu Pro Arg
20 25 30
Glu Leu Phe
35
<210> 150
<211> 40
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 150
Pro Glu Pro Thr Ile Asp Glu Leu Leu Pro Arg Glu Leu Phe Pro Pro
1 5 10 15
Leu Phe Met Ala Ala Phe Asp Gly Arg His Ser Gln Thr Leu Lys Ala
20 25 30
Met Val Gln Ala Trp Pro Phe Thr
35 40
<210> 151
<211> 33
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 151
Leu Lys Ala Met Val Gln Ala Trp Pro Phe Thr Cys Leu Pro Leu Gly
1 5 10 15
Val Leu Met Lys Gly Gln His Leu His Leu Glu Thr Phe Lys Ala Val
20 25 30
Leu
<210> 152
<211> 35
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 152
Cys Leu Pro Leu Gly Val Leu Met Lys Gly Gln His Leu His Leu Glu
1 5 10 15
Thr Phe Lys Ala Val Leu Asp Gly Leu Asp Val Leu Leu Ala Gln Glu
20 25 30
Val Arg Pro
35
<210> 153
<211> 33
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 153
Leu Glu Thr Phe Lys Ala Val Leu Asp Gly Leu Asp Val Leu Leu Ala
1 5 10 15
Gln Glu Val Arg Pro Arg Arg Trp Lys Leu Gln Val Leu Asp Leu Arg
20 25 30
Lys
<210> 154
<211> 33
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 154
Val Arg Pro Arg Arg Trp Lys Leu Gln Val Leu Asp Leu Arg Lys Asn
1 5 10 15
Ser His Gln Asp Phe Trp Thr Val Trp Ser Gly Asn Arg Ala Ser Leu
20 25 30
Tyr
<210> 155
<211> 34
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 155
Trp Thr Val Trp Ser Gly Asn Arg Ala Ser Leu Tyr Ser Phe Pro Glu
1 5 10 15
Pro Glu Ala Ala Gln Pro Met Thr Lys Lys Arg Lys Val Asp Gly Leu
20 25 30
Ser Thr
<210> 156
<211> 35
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 156
Ile Pro Val Glu Val Leu Val Asp Leu Phe Leu Lys Glu Gly Ala Cys
1 5 10 15
Asp Glu Leu Phe Ser Tyr Leu Ile Glu Lys Val Lys Arg Lys Lys Asn
20 25 30
Val Leu Arg
35
<210> 157
<211> 34
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 157
Glu Leu Phe Ser Tyr Leu Ile Glu Lys Val Lys Arg Lys Lys Asn Val
1 5 10 15
Leu Arg Leu Cys Cys Lys Lys Leu Lys Ile Phe Ala Met Pro Met Gln
20 25 30
Asp Ile
<210> 158
<211> 35
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 158
Ser Ile Glu Asp Leu Glu Val Thr Cys Thr Trp Lys Leu Pro Thr Leu
1 5 10 15
Ala Lys Phe Ser Pro Tyr Leu Gly Gln Met Ile Asn Leu Arg Arg Leu
20 25 30
Leu Leu Ser
35
<210> 159
<211> 33
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 159
Pro Thr Leu Ala Lys Phe Ser Pro Tyr Leu Gly Gln Met Ile Asn Leu
1 5 10 15
Arg Arg Leu Leu Leu Ser His Ile His Ala Ser Ser Tyr Ile Ser Pro
20 25 30
Glu
<210> 160
<211> 33
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 160
Leu Arg Arg Leu Leu Leu Ser His Ile His Ala Ser Ser Tyr Ile Ser
1 5 10 15
Pro Glu Lys Glu Glu Gln Tyr Ile Ala Gln Phe Thr Ser Gln Phe Leu
20 25 30
Ser
<210> 161
<211> 33
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 161
Tyr Ile Ala Gln Phe Thr Ser Gln Phe Leu Ser Leu Gln Cys Leu Gln
1 5 10 15
Ala Leu Tyr Val Asp Ser Leu Phe Phe Leu Arg Gly Arg Leu Asp Gln
20 25 30
Leu
<210> 162
<211> 33
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 162
Leu Gln Cys Leu Gln Ala Leu Tyr Val Asp Ser Leu Phe Phe Leu Arg
1 5 10 15
Gly Arg Leu Asp Gln Leu Leu Arg His Val Met Asn Pro Leu Glu Thr
20 25 30
Leu
<210> 163
<211> 35
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 163
Val Leu Ser Leu Ser Gly Val Met Leu Thr Asp Val Ser Pro Glu Pro
1 5 10 15
Leu Gln Ala Leu Leu Glu Arg Ala Ser Ala Thr Leu Gln Asp Leu Val
20 25 30
Phe Asp Glu
35
<210> 164
<211> 33
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 164
Leu Pro Ser Leu Ser His Cys Ser Gln Leu Thr Thr Leu Ser Phe Tyr
1 5 10 15
Gly Asn Ser Ile Ser Ile Ser Ala Leu Gln Ser Leu Leu Gln His Leu
20 25 30
Ile
<210> 165
<211> 34
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 165
Ser Ile Ser Ile Ser Ala Leu Gln Ser Leu Leu Gln His Leu Ile Gly
1 5 10 15
Leu Ser Asn Leu Thr His Val Leu Tyr Pro Val Pro Leu Glu Ser Tyr
20 25 30
Glu Asp
<210> 166
<211> 34
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 166
Ser Tyr Glu Asp Ile His Gly Thr Leu His Leu Glu Arg Leu Ala Tyr
1 5 10 15
Leu His Ala Arg Leu Arg Glu Leu Leu Cys Glu Leu Gly Arg Pro Ser
20 25 30
Met Val
<210> 167
<211> 33
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 167
Pro Ser Met Val Trp Leu Ser Ala Asn Pro Cys Pro His Cys Gly Asp
1 5 10 15
Arg Thr Phe Tyr Asp Pro Glu Pro Ile Leu Cys Pro Cys Phe Met Pro
20 25 30
Asn
<210> 168
<211> 27
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 168
Met Glu Arg Arg Arg Leu Trp Gly Ser Ile Gln Ser Arg Tyr Ile Ser
1 5 10 15
Met Ser Val Trp Thr Ser Pro Arg Arg Leu Val
20 25
<210> 169
<211> 27
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 169
Val Trp Thr Ser Pro Arg Arg Leu Val Glu Leu Ala Gly Gln Ser Leu
1 5 10 15
Leu Lys Asp Glu Ala Leu Ala Ile Ala Ala Leu
20 25
<210> 170
<211> 22
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 170
Leu Pro Arg Glu Leu Phe Pro Pro Leu Phe Met Ala Ala Phe Asp Gly
1 5 10 15
Arg His Ser Gln Thr Leu
20
<210> 171
<211> 27
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 171
Phe Pro Pro Leu Phe Met Ala Ala Phe Asp Gly Arg His Ser Gln Thr
1 5 10 15
Leu Lys Ala Met Val Gln Ala Trp Pro Phe Thr
20 25
<210> 172
<211> 26
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 172
Lys Ala Met Val Gln Ala Trp Pro Phe Thr Cys Leu Pro Leu Gly Val
1 5 10 15
Leu Met Lys Gly Gln His Leu His Leu Glu
20 25
<210> 173
<211> 27
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 173
Gly Val Leu Met Lys Gly Gln His Leu His Leu Glu Thr Phe Lys Ala
1 5 10 15
Val Leu Asp Gly Leu Asp Val Leu Leu Ala Gln
20 25
<210> 174
<211> 27
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 174
Lys Ala Val Leu Asp Gly Leu Asp Val Leu Leu Ala Gln Glu Val Arg
1 5 10 15
Pro Arg Arg Trp Lys Leu Gln Val Leu Asp Leu
20 25
<210> 175
<211> 27
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 175
Arg Trp Lys Leu Gln Val Leu Asp Leu Arg Lys Asn Ser His Gln Asp
1 5 10 15
Phe Trp Thr Val Trp Ser Gly Asn Arg Ala Ser
20 25
<210> 176
<211> 27
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 176
Trp Thr Val Trp Ser Gly Asn Arg Ala Ser Leu Tyr Ser Phe Pro Glu
1 5 10 15
Pro Glu Ala Ala Gln Pro Met Thr Lys Lys Arg
20 25
<210> 177
<211> 27
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 177
Leu Phe Leu Lys Glu Gly Ala Cys Asp Glu Leu Phe Ser Tyr Leu Ile
1 5 10 15
Glu Lys Val Lys Arg Lys Lys Asn Val Leu Arg
20 25
<210> 178
<211> 27
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 178
Tyr Leu Ile Glu Lys Val Lys Arg Lys Lys Asn Val Leu Arg Leu Cys
1 5 10 15
Cys Lys Lys Leu Lys Ile Phe Ala Met Pro Met
20 25
<210> 179
<211> 22
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 179
Ser Ile Glu Asp Leu Glu Val Thr Cys Thr Trp Lys Leu Pro Thr Leu
1 5 10 15
Ala Lys Phe Ser Pro Tyr
20
<210> 180
<211> 27
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 180
Pro Thr Leu Ala Lys Phe Ser Pro Tyr Leu Gly Gln Met Ile Asn Leu
1 5 10 15
Arg Arg Leu Leu Leu Ser His Ile His Ala Ser
20 25
<210> 181
<211> 22
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 181
Leu Gly Gln Met Ile Asn Leu Arg Arg Leu Leu Leu Ser His Ile His
1 5 10 15
Ala Ser Ser Tyr Ile Ser
20
<210> 182
<211> 27
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 182
Leu Arg Arg Leu Leu Leu Ser His Ile His Ala Ser Ser Tyr Ile Ser
1 5 10 15
Pro Glu Lys Glu Glu Gln Tyr Ile Ala Gln Phe
20 25
<210> 183
<211> 27
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 183
Ser Gln Phe Leu Ser Leu Gln Cys Leu Gln Ala Leu Tyr Val Asp Ser
1 5 10 15
Leu Phe Phe Leu Arg Gly Arg Leu Asp Gln Leu
20 25
<210> 184
<211> 27
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 184
Ala Leu Tyr Val Asp Ser Leu Phe Phe Leu Arg Gly Arg Leu Asp Gln
1 5 10 15
Leu Leu Arg His Val Met Asn Pro Leu Glu Thr
20 25
<210> 185
<211> 27
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 185
Val Leu Ser Leu Ser Gly Val Met Leu Thr Asp Val Ser Pro Glu Pro
1 5 10 15
Leu Gln Ala Leu Leu Glu Arg Ala Ser Ala Thr
20 25
<210> 186
<211> 27
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 186
Leu Pro Ser Leu Ser His Cys Ser Gln Leu Thr Thr Leu Ser Phe Tyr
1 5 10 15
Gly Asn Ser Ile Ser Ile Ser Ala Leu Gln Ser
20 25
<210> 187
<211> 27
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 187
Gln Ser Leu Leu Gln His Leu Ile Gly Leu Ser Asn Leu Thr His Val
1 5 10 15
Leu Tyr Pro Val Pro Leu Glu Ser Tyr Glu Asp
20 25
<210> 188
<211> 27
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 188
Ser Tyr Glu Asp Ile His Gly Thr Leu His Leu Glu Arg Leu Ala Tyr
1 5 10 15
Leu His Ala Arg Leu Arg Glu Leu Leu Cys Glu
20 25
<210> 189
<211> 27
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 189
Ser Ala Asn Pro Cys Pro His Cys Gly Asp Arg Thr Phe Tyr Asp Pro
1 5 10 15
Glu Pro Ile Leu Cys Pro Cys Phe Met Pro Asn
20 25
<210> 190
<211> 393
<212> PRT
<213> Homo sapiens
<400> 190
Met Glu Glu Pro Gln Ser Asp Pro Ser Val Glu Pro Pro Leu Ser Gln
1 5 10 15
Glu Thr Phe Ser Asp Leu Trp Lys Leu Leu Pro Glu Asn Asn Val Leu
20 25 30
Ser Pro Leu Pro Ser Gln Ala Met Asp Asp Leu Met Leu Ser Pro Asp
35 40 45
Asp Ile Glu Gln Trp Phe Thr Glu Asp Pro Gly Pro Asp Glu Ala Pro
50 55 60
Arg Met Pro Glu Ala Ala Pro Pro Val Ala Pro Ala Pro Ala Ala Pro
65 70 75 80
Thr Pro Ala Ala Pro Ala Pro Ala Pro Ser Trp Pro Leu Ser Ser Ser
85 90 95
Val Pro Ser Gln Lys Thr Tyr Gln Gly Ser Tyr Gly Phe Arg Leu Gly
100 105 110
Phe Leu His Ser Gly Thr Ala Lys Ser Val Thr Cys Thr Tyr Ser Pro
115 120 125
Ala Leu Asn Lys Met Phe Cys Gln Leu Ala Lys Thr Cys Pro Val Gln
130 135 140
Leu Trp Val Asp Ser Thr Pro Pro Pro Gly Thr Arg Val Arg Ala Met
145 150 155 160
Ala Ile Tyr Lys Gln Ser Gln His Met Thr Glu Val Val Arg Arg Cys
165 170 175
Pro His His Glu Arg Cys Ser Asp Ser Asp Gly Leu Ala Pro Pro Gln
180 185 190
His Leu Ile Arg Val Glu Gly Asn Leu Arg Val Glu Tyr Leu Asp Asp
195 200 205
Arg Asn Thr Phe Arg His Ser Val Val Val Pro Tyr Glu Pro Pro Glu
210 215 220
Val Gly Ser Asp Cys Thr Thr Ile His Tyr Asn Tyr Met Cys Asn Ser
225 230 235 240
Ser Cys Met Gly Gly Met Asn Arg Arg Pro Ile Leu Thr Ile Ile Thr
245 250 255
Leu Glu Asp Ser Ser Gly Asn Leu Leu Gly Arg Asn Ser Phe Glu Val
260 265 270
Arg Val Cys Ala Cys Pro Gly Arg Asp Arg Arg Thr Glu Glu Glu Asn
275 280 285
Leu Arg Lys Lys Gly Glu Pro His His Glu Leu Pro Pro Gly Ser Thr
290 295 300
Lys Arg Ala Leu Pro Asn Asn Thr Ser Ser Ser Pro Gln Pro Lys Lys
305 310 315 320
Lys Pro Leu Asp Gly Glu Tyr Phe Thr Leu Gln Ile Arg Gly Arg Glu
325 330 335
Arg Phe Glu Met Phe Arg Glu Leu Asn Glu Ala Leu Glu Leu Lys Asp
340 345 350
Ala Gln Ala Gly Lys Glu Pro Gly Gly Ser Arg Ala His Ser Ser His
355 360 365
Leu Lys Ser Lys Lys Gly Gln Ser Thr Ser Arg His Lys Lys Leu Met
370 375 380
Phe Lys Thr Glu Gly Pro Asp Ser Asp
385 390
<210> 191
<211> 30
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 191
Ala Pro Ala Pro Ser Trp Pro Leu Ser Ser Ser Val Pro Ser Gln Lys
1 5 10 15
Thr Tyr Gln Gly Ser Tyr Gly Phe Arg Leu Gly Phe Leu His
20 25 30
<210> 192
<211> 30
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 192
Thr Tyr Gln Gly Ser Tyr Gly Phe Arg Leu Gly Phe Leu His Ser Gly
1 5 10 15
Thr Ala Lys Ser Val Thr Cys Thr Tyr Ser Pro Ala Leu Asn
20 25 30
<210> 193
<211> 30
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 193
Pro Val Gln Leu Trp Val Asp Ser Thr Pro Pro Pro Gly Thr Arg Val
1 5 10 15
Arg Ala Met Ala Ile Tyr Lys Gln Ser Gln His Met Thr Glu
20 25 30
<210> 194
<211> 30
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 194
Val Arg Ala Met Ala Ile Tyr Lys Gln Ser Gln His Met Thr Glu Val
1 5 10 15
Val Arg Arg Cys Pro His His Glu Arg Cys Ser Asp Ser Asp
20 25 30
<210> 195
<211> 30
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 195
Pro Pro Gln His Leu Ile Arg Val Glu Gly Asn Leu Arg Val Glu Tyr
1 5 10 15
Leu Asp Asp Arg Asn Thr Phe Arg His Ser Val Val Val Pro
20 25 30
<210> 196
<211> 25
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 196
Glu Val Gly Ser Asp Cys Thr Thr Ile His Tyr Asn Tyr Met Cys Asn
1 5 10 15
Ser Ser Cys Met Gly Gly Met Asn Arg
20 25
<210> 197
<211> 30
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 197
Val Gly Ser Asp Cys Thr Thr Ile His Tyr Asn Tyr Met Cys Asn Ser
1 5 10 15
Ser Cys Met Gly Gly Met Asn Arg Arg Pro Ile Leu Thr Ile
20 25 30
<210> 198
<211> 30
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 198
Leu Glu Asp Ser Ser Gly Asn Leu Leu Gly Arg Asn Ser Phe Glu Val
1 5 10 15
Arg Val Cys Ala Cys Pro Gly Arg Asp Arg Arg Thr Glu Glu
20 25 30
<210> 199
<211> 30
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 199
Arg Val Cys Ala Cys Pro Gly Arg Asp Arg Arg Thr Glu Glu Glu Asn
1 5 10 15
Leu Arg Lys Lys Gly Glu Pro His His Glu Leu Pro Pro Gly
20 25 30
<210> 200
<211> 30
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 200
Leu Asp Asp Arg Asn Thr Phe Arg His Ser Val Val Val Pro Tyr Glu
1 5 10 15
Pro Pro Glu Val Gly Ser Asp Cys Thr Thr Ile His Tyr Asn
20 25 30
<210> 201
<211> 30
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 201
Arg Arg Cys Pro His His Glu Arg Cys Ser Asp Ser Asp Gly Leu Ala
1 5 10 15
Pro Pro Gln His Leu Ile Arg Val Glu Gly Asn Leu Arg Val
20 25 30
<210> 202
<211> 30
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 202
Ser Cys Met Gly Gly Met Asn Arg Arg Pro Ile Leu Thr Ile Ile Thr
1 5 10 15
Leu Glu Asp Ser Ser Gly Asn Leu Leu Gly Arg Asn Ser Phe
20 25 30
<210> 203
<211> 30
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 203
Tyr Ser Pro Ala Leu Asn Lys Met Phe Cys Gln Leu Ala Lys Thr Cys
1 5 10 15
Pro Val Gln Leu Trp Val Asp Ser Thr Pro Pro Pro Gly Thr
20 25 30
<210> 204
<211> 30
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 204
Ala Pro Pro Val Ala Pro Ala Pro Ala Ala Pro Thr Pro Ala Ala Pro
1 5 10 15
Ala Pro Ala Pro Ser Trp Pro Leu Ser Ser Ser Val Pro Ser
20 25 30
<210> 205
<211> 30
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 205
Ile Tyr Lys Gln Ser Gln His Met Thr Glu Val Val Arg Arg Cys Pro
1 5 10 15
His His Glu Arg Cys Ser Asp Ser Asp Gly Leu Ala Pro Pro
20 25 30
<210> 206
<211> 30
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 206
Lys Arg Ala Leu Pro Asn Asn Thr Ser Ser Ser Pro Gln Pro Lys Lys
1 5 10 15
Lys Pro Leu Asp Gly Glu Tyr Phe Thr Leu Gln Ile Arg Gly
20 25 30
<210> 207
<211> 30
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 207
Ala Gln Ala Gly Lys Glu Pro Gly Gly Ser Arg Ala His Ser Ser His
1 5 10 15
Leu Lys Ser Lys Lys Gly Gln Ser Thr Ser Arg His Lys Lys
20 25 30
<210> 208
<211> 25
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 208
Leu Lys Ser Lys Lys Gly Gln Ser Thr Ser Arg His Lys Lys Leu Met
1 5 10 15
Phe Lys Thr Glu Gly Pro Asp Ser Asp
20 25
<210> 209
<211> 30
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 209
Leu Arg Lys Lys Gly Glu Pro His His Glu Leu Pro Pro Gly Ser Thr
1 5 10 15
Lys Arg Ala Leu Pro Asn Asn Thr Ser Ser Ser Pro Gln Pro
20 25 30
<210> 210
<211> 30
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 210
Lys Pro Leu Asp Gly Glu Tyr Phe Thr Leu Gln Ile Arg Gly Arg Glu
1 5 10 15
Arg Phe Glu Met Phe Arg Glu Leu Asn Glu Ala Leu Glu Leu
20 25 30
<210> 211
<211> 30
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 211
Arg Phe Glu Met Phe Arg Glu Leu Asn Glu Ala Leu Glu Leu Lys Asp
1 5 10 15
Ala Gln Ala Gly Lys Glu Pro Gly Gly Ser Arg Ala His Ser
20 25 30
<210> 212
<211> 720
<212> PRT
<213> Homo sapiens
<400> 212
Met Trp Asn Leu Leu His Glu Thr Asp Ser Ala Val Ala Thr Ala Arg
1 5 10 15
Arg Pro Arg Trp Leu Cys Ala Gly Ala Leu Val Leu Ala Gly Gly Phe
20 25 30
Phe Leu Leu Gly Phe Leu Phe Gly Trp Phe Ile Lys Ser Ser Asn Glu
35 40 45
Ala Thr Asn Ile Thr Pro Lys His Asn Met Lys Ala Phe Leu Asp Glu
50 55 60
Leu Lys Ala Glu Asn Ile Lys Lys Phe Leu Tyr Asn Phe Thr Gln Ile
65 70 75 80
Pro His Leu Ala Gly Thr Glu Gln Asn Phe Gln Leu Ala Lys Gln Ile
85 90 95
Gln Ser Gln Trp Lys Glu Phe Gly Leu Asp Ser Val Glu Leu Ala His
100 105 110
Tyr Asp Val Leu Leu Ser Tyr Pro Asn Lys Thr His Pro Asn Tyr Ile
115 120 125
Ser Ile Ile Asn Glu Asp Gly Asn Glu Ile Phe Asn Thr Ser Leu Phe
130 135 140
Glu Pro Pro Pro Pro Gly Tyr Glu Asn Val Ser Asp Ile Val Pro Pro
145 150 155 160
Phe Ser Ala Phe Ser Pro Gln Gly Met Pro Glu Gly Asp Leu Val Tyr
165 170 175
Val Asn Tyr Ala Arg Thr Glu Asp Phe Phe Lys Leu Glu Arg Asp Met
180 185 190
Lys Ile Asn Cys Ser Gly Lys Ile Val Ile Ala Arg Tyr Gly Lys Val
195 200 205
Phe Arg Gly Asn Lys Val Lys Asn Ala Gln Leu Ala Gly Ala Lys Gly
210 215 220
Val Ile Leu Tyr Ser Asp Pro Ala Asp Tyr Phe Ala Pro Gly Val Lys
225 230 235 240
Ser Tyr Pro Asp Gly Trp Asn Leu Pro Gly Gly Gly Val Gln Arg Gly
245 250 255
Asn Ile Leu Asn Leu Asn Gly Ala Gly Asp Pro Leu Thr Pro Gly Tyr
260 265 270
Pro Ala Asn Glu Tyr Ala Tyr Arg Arg Gly Ile Ala Glu Ala Val Gly
275 280 285
Leu Pro Ser Ile Pro Val His Pro Ile Gly Tyr Tyr Asp Ala Gln Lys
290 295 300
Leu Leu Glu Lys Met Gly Gly Ser Ala Pro Pro Asp Ser Ser Trp Arg
305 310 315 320
Gly Ser Leu Lys Val Pro Tyr Asn Val Gly Pro Gly Phe Thr Gly Asn
325 330 335
Phe Ser Thr Gln Lys Val Lys Met His Ile His Ser Thr Asn Glu Val
340 345 350
Thr Arg Ile Tyr Asn Val Ile Gly Thr Leu Arg Gly Ala Val Glu Pro
355 360 365
Asp Arg Tyr Val Ile Leu Gly Gly His Arg Asp Ser Trp Val Phe Gly
370 375 380
Gly Ile Asp Pro Gln Ser Gly Ala Ala Val Val His Glu Ile Val Arg
385 390 395 400
Ser Phe Gly Thr Leu Lys Lys Glu Gly Trp Arg Pro Arg Arg Thr Ile
405 410 415
Leu Phe Ala Ser Trp Asp Ala Glu Glu Phe Gly Leu Leu Gly Ser Thr
420 425 430
Glu Trp Ala Glu Glu Asn Ser Arg Leu Leu Gln Glu Arg Gly Val Ala
435 440 445
Tyr Ile Asn Ala Asp Ser Ser Ile Glu Gly Asn Tyr Thr Leu Arg Val
450 455 460
Asp Cys Thr Pro Leu Met Tyr Ser Leu Val His Asn Leu Thr Lys Glu
465 470 475 480
Leu Lys Ser Pro Asp Glu Gly Phe Glu Gly Lys Ser Leu Tyr Glu Ser
485 490 495
Trp Thr Lys Lys Ser Pro Ser Pro Glu Phe Ser Gly Met Pro Arg Ile
500 505 510
Ser Lys Leu Gly Ser Gly Asn Asp Phe Glu Val Phe Phe Gln Arg Leu
515 520 525
Gly Ile Ala Ser Gly Arg Ala Arg Tyr Thr Lys Asn Trp Glu Thr Asn
530 535 540
Lys Phe Ser Gly Tyr Pro Leu Tyr His Ser Val Tyr Glu Thr Tyr Glu
545 550 555 560
Leu Val Glu Lys Phe Tyr Asp Pro Met Phe Lys Tyr His Leu Thr Val
565 570 575
Ala Gln Val Arg Gly Gly Met Val Phe Glu Leu Ala Asn Ser Ile Val
580 585 590
Leu Pro Phe Asp Cys Arg Asp Tyr Ala Val Val Leu Arg Lys Tyr Ala
595 600 605
Asp Lys Ile Tyr Ser Ile Ser Met Lys His Pro Gln Glu Met Lys Thr
610 615 620
Tyr Ser Val Ser Phe Asp Ser Leu Phe Ser Ala Val Lys Asn Phe Thr
625 630 635 640
Glu Ile Ala Ser Lys Phe Ser Glu Arg Leu Gln Asp Phe Asp Lys Ser
645 650 655
Asn Pro Ile Val Leu Arg Met Met Asn Asp Gln Leu Met Phe Leu Glu
660 665 670
Arg Ala Phe Ile Asp Pro Leu Gly Leu Pro Asp Arg Pro Phe Tyr Arg
675 680 685
His Val Ile Tyr Ala Pro Ser Ser His Asn Lys Tyr Ala Gly Glu Ser
690 695 700
Phe Pro Gly Ile Tyr Asp Ala Leu Phe Asp Ile Glu Ser Lys Val Asp
705 710 715 720
<210> 213
<211> 33
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 213
Asn Leu Leu His Glu Thr Asp Ser Ala Val Ala Thr Ala Arg Arg Pro
1 5 10 15
Arg Trp Leu Cys Ala Gly Ala Leu Val Leu Ala Gly Gly Phe Phe Leu
20 25 30
Leu
<210> 214
<211> 35
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 214
Gly Phe Phe Leu Leu Gly Phe Leu Phe Gly Trp Phe Ile Lys Ser Ser
1 5 10 15
Asn Glu Ala Thr Asn Ile Thr Pro Lys His Asn Met Lys Ala Phe Leu
20 25 30
Asp Glu Leu
35
<210> 215
<211> 36
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 215
Thr Pro Lys His Asn Met Lys Ala Phe Leu Asp Glu Leu Lys Ala Glu
1 5 10 15
Asn Ile Lys Lys Phe Leu Tyr Asn Phe Thr Gln Ile Pro His Leu Ala
20 25 30
Gly Thr Glu Gln
35
<210> 216
<211> 37
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 216
Lys Gln Ile Gln Ser Gln Trp Lys Glu Phe Gly Leu Asp Ser Val Glu
1 5 10 15
Leu Ala His Tyr Asp Val Leu Leu Ser Tyr Pro Asn Lys Thr His Pro
20 25 30
Asn Tyr Ile Ser Ile
35
<210> 217
<211> 33
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 217
Asp Ile Val Pro Pro Phe Ser Ala Phe Ser Pro Gln Gly Met Pro Glu
1 5 10 15
Gly Asp Leu Val Tyr Val Asn Tyr Ala Arg Thr Glu Asp Phe Phe Lys
20 25 30
Leu
<210> 218
<211> 36
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 218
Lys Val Phe Arg Gly Asn Lys Val Lys Asn Ala Gln Leu Ala Gly Ala
1 5 10 15
Lys Gly Val Ile Leu Tyr Ser Asp Pro Ala Asp Tyr Phe Ala Pro Gly
20 25 30
Val Lys Ser Tyr
35
<210> 219
<211> 37
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 219
Val Gln Arg Gly Asn Ile Leu Asn Leu Asn Gly Ala Gly Asp Pro Leu
1 5 10 15
Thr Pro Gly Tyr Pro Ala Asn Glu Tyr Ala Tyr Arg Arg Gly Ile Ala
20 25 30
Glu Ala Val Gly Leu
35
<210> 220
<211> 32
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 220
Ala Gln Lys Leu Leu Glu Lys Met Gly Gly Ser Ala Pro Pro Asp Ser
1 5 10 15
Ser Trp Arg Gly Ser Leu Lys Val Pro Tyr Asn Val Gly Pro Gly Phe
20 25 30
<210> 221
<211> 31
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 221
Lys Val Lys Met His Ile His Ser Thr Asn Glu Val Thr Arg Ile Tyr
1 5 10 15
Asn Val Ile Gly Thr Leu Arg Gly Ala Val Glu Pro Asp Arg Tyr
20 25 30
<210> 222
<211> 34
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 222
Ala Val Val His Glu Ile Val Arg Ser Phe Gly Thr Leu Lys Lys Glu
1 5 10 15
Gly Trp Arg Pro Arg Arg Thr Ile Leu Phe Ala Ser Trp Asp Ala Glu
20 25 30
Glu Phe
<210> 223
<211> 33
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 223
Thr Glu Trp Ala Glu Glu Asn Ser Arg Leu Leu Gln Glu Arg Gly Val
1 5 10 15
Ala Tyr Ile Asn Ala Asp Ser Ser Ile Glu Gly Asn Tyr Thr Leu Arg
20 25 30
Val
<210> 224
<211> 35
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 224
Asn Ala Asp Ser Ser Ile Glu Gly Asn Tyr Thr Leu Arg Val Asp Cys
1 5 10 15
Thr Pro Leu Met Tyr Ser Leu Val His Asn Leu Thr Lys Glu Leu Lys
20 25 30
Ser Pro Asp
35
<210> 225
<211> 32
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 225
Leu Met Tyr Ser Leu Val His Asn Leu Thr Lys Glu Leu Lys Ser Pro
1 5 10 15
Asp Glu Gly Phe Glu Gly Lys Ser Leu Tyr Glu Ser Trp Thr Lys Lys
20 25 30
<210> 226
<211> 33
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 226
Ser Gly Met Pro Arg Ile Ser Lys Leu Gly Ser Gly Asn Asp Phe Glu
1 5 10 15
Val Phe Phe Gln Arg Leu Gly Ile Ala Ser Gly Arg Ala Arg Tyr Thr
20 25 30
Lys
<210> 227
<211> 33
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 227
Ser Gly Tyr Pro Leu Tyr His Ser Val Tyr Glu Thr Tyr Glu Leu Val
1 5 10 15
Glu Lys Phe Tyr Asp Pro Met Phe Lys Tyr His Leu Thr Val Ala Gln
20 25 30
Val
<210> 228
<211> 36
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 228
Phe Tyr Asp Pro Met Phe Lys Tyr His Leu Thr Val Ala Gln Val Arg
1 5 10 15
Gly Gly Met Val Phe Glu Leu Ala Asn Ser Ile Val Leu Pro Phe Asp
20 25 30
Cys Arg Asp Tyr
35
<210> 229
<211> 34
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 229
Val Leu Arg Lys Tyr Ala Asp Lys Ile Tyr Ser Ile Ser Met Lys His
1 5 10 15
Pro Gln Glu Met Lys Thr Tyr Ser Val Ser Phe Asp Ser Leu Phe Ser
20 25 30
Ala Val
<210> 230
<211> 34
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 230
Glu Arg Leu Gln Asp Phe Asp Lys Ser Asn Pro Ile Val Leu Arg Met
1 5 10 15
Met Asn Asp Gln Leu Met Phe Leu Glu Arg Ala Phe Ile Asp Pro Leu
20 25 30
Gly Leu
<210> 231
<211> 35
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 231
Leu Gly Leu Pro Asp Arg Pro Phe Tyr Arg His Val Ile Tyr Ala Pro
1 5 10 15
Ser Ser His Asn Lys Tyr Ala Gly Glu Ser Phe Pro Gly Ile Tyr Asp
20 25 30
Ala Leu Phe
35
<210> 232
<211> 34
<212> PRT
<213> Artificial
<220>
<223> peptide
<400> 232
Glu Ser Lys Val Asp Pro Ser Lys Ala Trp Gly Glu Val Lys Arg Gln
1 5 10 15
Ile Tyr Val Ala Ala Phe Thr Val Gln Ala Ala Ala Glu Thr Leu Ser
20 25 30
Glu Val
Claims (10)
- i) SEQ ID NO: 1-5로부터 선택된 서열을 포함하거나 이로 구성된 5개의 펩타이드; 또는
ii) SEQ ID NO: 1-6으로 표시되는 서열을 포함하거나 이로 구성된 6개의 펩타이드; 또는
iii) SEQ ID NO: 7-13으로 표시되는 서열을 포함하거나 이로 구성된 7개의 펩타이드
를 포함하거나 이로 구성된 펩타이드 혼합물(mix of peptides).
- 제1항에 있어서,
혼합물은 동결건조된 펩타이드 혼합물.
- 제1항 또는 제2항에 있어서,
펩타이드는 SEQ ID NO: 1-5로 표시되는 5개의 상이한 펩타이드들의 혼합물로 구성되는 펩타이드 혼합물.
- 제1항 또는 제2항에 있어서,
펩타이드는 SEQ ID NO: 7-13으로 표시되는 7개의 상이한 펩타이드들의 혼합물로 구성되는 펩타이드 혼합물.
- 제1항 또는 제2항에 있어서,
혼합물 내의 상이한 펩타이드들이 실질적으로 동일한 비율로 존재하는 펩타이드 혼합물.
- 제1항 또는 제2항에 있어서,
혼합물은
i) SEQ ID NO: 1-5로부터 선택된 서열을 포함하거나 이로 구성된 5개의 펩타이드; 또는
ii) SEQ ID NO: 1-6으로 표시되는 서열을 포함하거나 이로 구성된 6개의 펩타이드; 또는
iii) SEQ ID NO: 7-13으로 표시되는 서열을 포함하거나 이로 구성된 7개의 펩타이드
로 구성되는 펩타이드 혼합물.
- 제1항 또는 제2항에 있어서,
혼합물은
i) SEQ ID NO: 1-5에서 선택된 서열로 구성된 5개의 펩타이드; 또는
ii) SEQ ID NO: 1-6으로 표시되는 서열로 구성된 6개의 펩타이드; 또는
iii) SEQ ID NO: 7-13으로 표시되는 서열로 구성된 7개의 펩타이드
를 포함하거나 이로 구성되는 펩타이드 혼합물.
- 제1항 또는 제2항에 있어서,
혼합물은
i) SEQ ID NO: 1-5에서 선택된 서열로 구성된 5개의 펩타이드; 또는
ii) SEQ ID NO: 1-6으로 표시되는 서열로 구성된 6개의 펩타이드; 또는
iii) SEQ ID NO: 7-13으로 표시되는 서열로 구성된 7개의 펩타이드
로 구성되는 펩타이드 혼합물.
- i) SEQ ID NO: 1-5 또는 SEQ ID NO: 1-6으로 표시되는 상이한 펩타이드들의 혼합물을 포함하는 제1 샷; 및
ii) SEQ ID NOs: 7-13으로 표시되는 상이한 펩타이드들의 혼합물을 포함하는 제2 샷
을 포함하는 약학적 투여 단위.
- 제9항에 있어서,
의약으로서 사용하기 위한 약학적 투여 단위로서, 의약은 바람직하게 백신이고, 더욱 바람직하게 의약은 상기 펩타이드들의 적어도 하나의 에피토프에 대한 T 세포 반응을 유도하기 위한 백신인 약학적 투여 단위.
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EP16175215 | 2016-06-20 | ||
PCT/EP2017/064882 WO2017220463A1 (en) | 2016-06-20 | 2017-06-19 | Formulation of a peptide vaccine |
KR1020197001793A KR20190020098A (ko) | 2016-06-20 | 2017-06-19 | 펩타이드 백신의 제형 |
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KR1020197001793A KR20190020098A (ko) | 2016-06-20 | 2017-06-19 | 펩타이드 백신의 제형 |
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KR1020197001793A KR20190020098A (ko) | 2016-06-20 | 2017-06-19 | 펩타이드 백신의 제형 |
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US (3) | US10702598B2 (ko) |
EP (2) | EP3471758A1 (ko) |
JP (2) | JP7115803B2 (ko) |
KR (2) | KR20230030032A (ko) |
CN (2) | CN109641039B (ko) |
AU (2) | AU2017281389B2 (ko) |
CA (1) | CA3027459A1 (ko) |
EA (1) | EA201990071A1 (ko) |
IL (2) | IL291537B2 (ko) |
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SG11201811442UA (en) | 2019-01-30 |
CA3027459A1 (en) | 2017-12-28 |
CN117018170A (zh) | 2023-11-10 |
MX2023003875A (es) | 2023-04-18 |
IL263846A (en) | 2019-01-31 |
EA201990071A1 (ru) | 2019-06-28 |
EP3552623A1 (en) | 2019-10-16 |
IL291537B2 (en) | 2023-11-01 |
AU2017281389B2 (en) | 2024-02-22 |
US20230233658A1 (en) | 2023-07-27 |
EP3471758A1 (en) | 2019-04-24 |
CN109641039A (zh) | 2019-04-16 |
IL291537A (en) | 2022-05-01 |
MY189551A (en) | 2022-02-16 |
AU2024202005A1 (en) | 2024-04-18 |
US20190231863A1 (en) | 2019-08-01 |
JP2022141878A (ja) | 2022-09-29 |
MX2018015749A (es) | 2019-06-17 |
US20200297835A1 (en) | 2020-09-24 |
AU2017281389A1 (en) | 2019-02-07 |
JP7115803B2 (ja) | 2022-08-09 |
WO2017220463A1 (en) | 2017-12-28 |
JP2019525950A (ja) | 2019-09-12 |
IL263846B (en) | 2022-04-01 |
CN109641039B (zh) | 2023-08-04 |
US10702598B2 (en) | 2020-07-07 |
US11426458B2 (en) | 2022-08-30 |
IL291537B1 (en) | 2023-07-01 |
ZA202100578B (en) | 2023-03-29 |
KR20190020098A (ko) | 2019-02-27 |
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