JP2008521869A5 - - Google Patents
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- JP2008521869A5 JP2008521869A5 JP2007543909A JP2007543909A JP2008521869A5 JP 2008521869 A5 JP2008521869 A5 JP 2008521869A5 JP 2007543909 A JP2007543909 A JP 2007543909A JP 2007543909 A JP2007543909 A JP 2007543909A JP 2008521869 A5 JP2008521869 A5 JP 2008521869A5
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- JP
- Japan
- Prior art keywords
- xaa
- seq
- dom7r
- glu
- lys
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
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- 125000003275 alpha amino acid group Chemical group 0.000 description 43
- 230000004927 fusion Effects 0.000 description 30
- 101001076407 Homo sapiens Interleukin-1 receptor antagonist protein Proteins 0.000 description 28
- 229940119178 Interleukin 1 receptor antagonist Drugs 0.000 description 26
- 102000051628 Interleukin-1 receptor antagonist Human genes 0.000 description 26
- 239000003407 interleukin 1 receptor blocking agent Substances 0.000 description 26
- 102000007562 Serum Albumin Human genes 0.000 description 15
- 108010071390 Serum Albumin Proteins 0.000 description 15
- 238000010586 diagram Methods 0.000 description 14
- 229940024606 amino acid Drugs 0.000 description 12
- 150000001408 amides Chemical class 0.000 description 11
- 150000001413 amino acids Chemical class 0.000 description 11
- 241000699666 Mus <mouse, genus> Species 0.000 description 10
- 239000002773 nucleotide Substances 0.000 description 10
- 125000003729 nucleotide group Chemical group 0.000 description 10
- FUOOLUPWFVMBKG-UHFFFAOYSA-N 2-Aminoisobutyric acid Chemical compound CC(C)(N)C(O)=O FUOOLUPWFVMBKG-UHFFFAOYSA-N 0.000 description 8
- DTHNMHAUYICORS-KTKZVXAJSA-N Glucagon-like peptide 1 Chemical class C([C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCCN)C(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(N)=O)NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@@H](N)CC=1N=CNC=1)[C@@H](C)O)[C@@H](C)O)C(C)C)C1=CC=CC=C1 DTHNMHAUYICORS-KTKZVXAJSA-N 0.000 description 8
- 102000008100 Human Serum Albumin Human genes 0.000 description 7
- 108091006905 Human Serum Albumin Proteins 0.000 description 7
- 108010084592 Saporins Proteins 0.000 description 7
- 210000002966 serum Anatomy 0.000 description 7
- 101710198884 GATA-type zinc finger protein 1 Proteins 0.000 description 6
- 102400000322 Glucagon-like peptide 1 Human genes 0.000 description 6
- 231100000673 dose–response relationship Toxicity 0.000 description 6
- 229940079593 drug Drugs 0.000 description 6
- 239000003814 drug Substances 0.000 description 6
- 108090000765 processed proteins & peptides Proteins 0.000 description 6
- 102000004890 Interleukin-8 Human genes 0.000 description 5
- 108090001007 Interleukin-8 Proteins 0.000 description 5
- 108010076504 Protein Sorting Signals Proteins 0.000 description 5
- 239000002243 precursor Substances 0.000 description 5
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 4
- -1 Nα-acetyl-histidine Chemical compound 0.000 description 4
- 238000002965 ELISA Methods 0.000 description 3
- HVLSXIKZNLPZJJ-TXZCQADKSA-N HA peptide Chemical compound C([C@@H](C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C(C)C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](C)C(O)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=C(O)C=C1 HVLSXIKZNLPZJJ-TXZCQADKSA-N 0.000 description 3
- 125000000539 amino acid group Chemical group 0.000 description 3
- 229960002885 histidine Drugs 0.000 description 3
- ZAHQPTJLOCWVPG-UHFFFAOYSA-N mitoxantrone dihydrochloride Chemical compound Cl.Cl.O=C1C2=C(O)C=CC(O)=C2C(=O)C2=C1C(NCCNCCO)=CC=C2NCCNCCO ZAHQPTJLOCWVPG-UHFFFAOYSA-N 0.000 description 3
- 108020004707 nucleic acids Proteins 0.000 description 3
- 102000039446 nucleic acids Human genes 0.000 description 3
- 150000007523 nucleic acids Chemical class 0.000 description 3
- 229920001184 polypeptide Polymers 0.000 description 3
- 102000004196 processed proteins & peptides Human genes 0.000 description 3
- 102000004169 proteins and genes Human genes 0.000 description 3
- 108090000623 proteins and genes Proteins 0.000 description 3
- CNMAQBJBWQQZFZ-LURJTMIESA-N (2s)-2-(pyridin-2-ylamino)propanoic acid Chemical compound OC(=O)[C@H](C)NC1=CC=CC=N1 CNMAQBJBWQQZFZ-LURJTMIESA-N 0.000 description 2
- WTKYBFQVZPCGAO-LURJTMIESA-N (2s)-2-(pyridin-3-ylamino)propanoic acid Chemical compound OC(=O)[C@H](C)NC1=CC=CN=C1 WTKYBFQVZPCGAO-LURJTMIESA-N 0.000 description 2
- SAAQPSNNIOGFSQ-LURJTMIESA-N (2s)-2-(pyridin-4-ylamino)propanoic acid Chemical compound OC(=O)[C@H](C)NC1=CC=NC=C1 SAAQPSNNIOGFSQ-LURJTMIESA-N 0.000 description 2
- AJFGLTPLWPTALJ-SSDOTTSWSA-N (2s)-2-azaniumyl-2-(fluoromethyl)-3-(1h-imidazol-5-yl)propanoate Chemical compound FC[C@@](N)(C(O)=O)CC1=CN=CN1 AJFGLTPLWPTALJ-SSDOTTSWSA-N 0.000 description 2
- MSECZMWQBBVGEN-LURJTMIESA-N (2s)-2-azaniumyl-4-(1h-imidazol-5-yl)butanoate Chemical compound OC(=O)[C@@H](N)CCC1=CN=CN1 MSECZMWQBBVGEN-LURJTMIESA-N 0.000 description 2
- UYEGXSNFZXWSDV-BYPYZUCNSA-N (2s)-3-(2-amino-1h-imidazol-5-yl)-2-azaniumylpropanoate Chemical compound OC(=O)[C@@H](N)CC1=CNC(N)=N1 UYEGXSNFZXWSDV-BYPYZUCNSA-N 0.000 description 2
- FVTVMQPGKVHSEY-UHFFFAOYSA-N 1-AMINOCYCLOBUTANE CARBOXYLIC ACID Chemical compound OC(=O)C1(N)CCC1 FVTVMQPGKVHSEY-UHFFFAOYSA-N 0.000 description 2
- IINRZEIPFQHEAP-UHFFFAOYSA-N 1-aminocycloheptane-1-carboxylic acid Chemical compound OC(=O)C1(N)CCCCCC1 IINRZEIPFQHEAP-UHFFFAOYSA-N 0.000 description 2
- PAJPWUMXBYXFCZ-UHFFFAOYSA-N 1-aminocyclopropanecarboxylic acid Chemical compound OC(=O)C1(N)CC1 PAJPWUMXBYXFCZ-UHFFFAOYSA-N 0.000 description 2
- PJSQECUPWDUIBT-UHFFFAOYSA-N 1-azaniumylcyclooctane-1-carboxylate Chemical compound OC(=O)C1(N)CCCCCCC1 PJSQECUPWDUIBT-UHFFFAOYSA-N 0.000 description 2
- 241000283707 Capra Species 0.000 description 2
- HNDVDQJCIGZPNO-RXMQYKEDSA-N D-histidine Chemical compound OC(=O)[C@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-RXMQYKEDSA-N 0.000 description 2
- 229930195721 D-histidine Natural products 0.000 description 2
- 108010011459 Exenatide Proteins 0.000 description 2
- 208000009386 Experimental Arthritis Diseases 0.000 description 2
- 102000000589 Interleukin-1 Human genes 0.000 description 2
- 108010002352 Interleukin-1 Proteins 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 102000001708 Protein Isoforms Human genes 0.000 description 2
- 108010029485 Protein Isoforms Proteins 0.000 description 2
- 206010003246 arthritis Diseases 0.000 description 2
- 150000001732 carboxylic acid derivatives Chemical class 0.000 description 2
- JUFFVKRROAPVBI-PVOYSMBESA-N chembl1210015 Chemical compound C([C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(=O)N[C@H]1[C@@H]([C@@H](O)[C@H](O[C@H]2[C@@H]([C@@H](O)[C@@H](O)[C@@H](CO[C@]3(O[C@@H](C[C@H](O)[C@H](O)CO)[C@H](NC(C)=O)[C@@H](O)C3)C(O)=O)O2)O)[C@@H](CO)O1)NC(C)=O)C(=O)NCC(=O)NCC(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)N1[C@@H](CCC1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CO)C(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCSC)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)CNC(=O)[C@@H](N)CC=1NC=NC=1)[C@@H](C)O)[C@@H](C)O)C(C)C)C1=CC=CC=C1 JUFFVKRROAPVBI-PVOYSMBESA-N 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- ZCKYOWGFRHAZIQ-UHFFFAOYSA-N dihydrourocanic acid Chemical compound OC(=O)CCC1=CNC=N1 ZCKYOWGFRHAZIQ-UHFFFAOYSA-N 0.000 description 2
- 229960001519 exenatide Drugs 0.000 description 2
- 108020001507 fusion proteins Proteins 0.000 description 2
- 102000037865 fusion proteins Human genes 0.000 description 2
- 230000005764 inhibitory process Effects 0.000 description 2
- 238000002347 injection Methods 0.000 description 2
- 239000007924 injection Substances 0.000 description 2
- 238000001990 intravenous administration Methods 0.000 description 2
- 230000028327 secretion Effects 0.000 description 2
- MPVGZUDRATZEEE-YFKPBYRVSA-N (2s)-2-amino-3-(3-hydroxyimidazol-4-yl)propanoic acid Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1O MPVGZUDRATZEEE-YFKPBYRVSA-N 0.000 description 1
- KQMBIBBJWXGSEI-ROLXFIACSA-N (2s)-2-amino-3-hydroxy-3-(1h-imidazol-5-yl)propanoic acid Chemical compound OC(=O)[C@@H](N)C(O)C1=CNC=N1 KQMBIBBJWXGSEI-ROLXFIACSA-N 0.000 description 1
- WOXWUZCRWJWTRT-UHFFFAOYSA-N 1-amino-1-cyclohexanecarboxylic acid Chemical compound OC(=O)C1(N)CCCCC1 WOXWUZCRWJWTRT-UHFFFAOYSA-N 0.000 description 1
- NILQLFBWTXNUOE-UHFFFAOYSA-N 1-aminocyclopentanecarboxylic acid Chemical compound OC(=O)C1(N)CCCC1 NILQLFBWTXNUOE-UHFFFAOYSA-N 0.000 description 1
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 description 1
- 108091035707 Consensus sequence Proteins 0.000 description 1
- 238000012286 ELISA Assay Methods 0.000 description 1
- 108010008165 Etanercept Proteins 0.000 description 1
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 1
- 102000003814 Interleukin-10 Human genes 0.000 description 1
- 108090000174 Interleukin-10 Proteins 0.000 description 1
- 125000000998 L-alanino group Chemical group [H]N([*])[C@](C([H])([H])[H])([H])C(=O)O[H] 0.000 description 1
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 1
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- 108700026244 Open Reading Frames Proteins 0.000 description 1
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 1
- HRRYYCWYCMJNGA-ZETCQYMHSA-N alpha-methyl-L-histidine Chemical compound OC(=O)[C@](N)(C)CC1=CN=CN1 HRRYYCWYCMJNGA-ZETCQYMHSA-N 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- UREBDLICKHMUKA-CXSFZGCWSA-N dexamethasone Chemical compound C1CC2=CC(=O)C=C[C@]2(C)[C@]2(F)[C@@H]1[C@@H]1C[C@@H](C)[C@@](C(=O)CO)(O)[C@@]1(C)C[C@@H]2O UREBDLICKHMUKA-CXSFZGCWSA-N 0.000 description 1
- 229960003957 dexamethasone Drugs 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 229940073621 enbrel Drugs 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 102000046824 human IL1RN Human genes 0.000 description 1
- 230000003914 insulin secretion Effects 0.000 description 1
- 229940076144 interleukin-10 Drugs 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 238000002864 sequence alignment Methods 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 150000003431 steroids Chemical class 0.000 description 1
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US63236104P | 2004-12-02 | 2004-12-02 | |
| US60/632,361 | 2004-12-02 | ||
| GB0511019.2 | 2005-05-31 | ||
| GB0511019A GB0511019D0 (en) | 2005-05-31 | 2005-05-31 | Drug fusions and conjugates |
| PCT/GB2005/004599 WO2006059106A2 (en) | 2004-12-02 | 2005-11-30 | Bispecific domain antibodies targeting serum albumin and glp-1 or pyy |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2008521869A JP2008521869A (ja) | 2008-06-26 |
| JP2008521869A5 true JP2008521869A5 (enExample) | 2008-10-23 |
| JP5185624B2 JP5185624B2 (ja) | 2013-04-17 |
Family
ID=40904147
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2007543909A Expired - Fee Related JP5185624B2 (ja) | 2004-12-02 | 2005-11-30 | 血清アルブミンおよびｇｌｐ−１またはｐｙｙを標的とする二重特異性抗体 |
Country Status (16)
| Country | Link |
|---|---|
| US (1) | US20090214534A1 (enExample) |
| EP (2) | EP2769990A3 (enExample) |
| JP (1) | JP5185624B2 (enExample) |
| KR (1) | KR20070094909A (enExample) |
| CN (1) | CN101128487B (enExample) |
| AU (1) | AU2005311099B2 (enExample) |
| BR (1) | BRPI0518761A2 (enExample) |
| CA (1) | CA2589800A1 (enExample) |
| IL (1) | IL183450A0 (enExample) |
| MA (1) | MA29079B1 (enExample) |
| MX (1) | MX2007006605A (enExample) |
| NO (1) | NO20072751L (enExample) |
| NZ (1) | NZ555464A (enExample) |
| RU (1) | RU2428431C2 (enExample) |
| SG (1) | SG157423A1 (enExample) |
| WO (1) | WO2006059106A2 (enExample) |
Families Citing this family (89)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7169752B2 (en) | 2003-09-30 | 2007-01-30 | New River Pharmaceuticals Inc. | Compounds and compositions for prevention of overdose of oxycodone |
| US20060014697A1 (en) | 2001-08-22 | 2006-01-19 | Travis Mickle | Pharmaceutical compositions for prevention of overdose or abuse |
| JP2005289809A (ja) | 2001-10-24 | 2005-10-20 | Vlaams Interuniversitair Inst Voor Biotechnologie Vzw (Vib Vzw) | 突然変異重鎖抗体 |
| US9321832B2 (en) * | 2002-06-28 | 2016-04-26 | Domantis Limited | Ligand |
| AU2006249144B2 (en) | 2005-05-18 | 2011-11-17 | Ablynx Nv | Improved NanobodiesTM against Tumor Necrosis Factor-alpha |
| DE102005023617A1 (de) | 2005-05-21 | 2006-11-23 | Aspre Ag | Verfahren zum Mischen von Farben in einem Display |
| EA013821B1 (ru) | 2005-05-25 | 2010-08-30 | Кьюрдм, Инк. | Проостровковые пептиды человека, их производные и аналоги и способы их применения |
| EP2471810A1 (en) * | 2006-02-22 | 2012-07-04 | Merck Sharp & Dohme Corporation | Oxyntomodulin derivatives |
| JP5252435B2 (ja) | 2006-03-15 | 2013-07-31 | ノボ・ノルデイスク・エー／エス | アミリン誘導体 |
| ES2534434T3 (es) | 2007-08-30 | 2015-04-22 | Curedm Group Holdings, Llc | Composiciones y métodos de uso de péptidos proislotes y análogos de los mismos |
| EP2036923A1 (en) * | 2007-09-11 | 2009-03-18 | Novo Nordisk A/S | Improved derivates of amylin |
| CA2701705A1 (en) * | 2007-10-08 | 2009-04-16 | Anaphore, Inc. | Trimeric il-1ra |
| KR20100132535A (ko) * | 2008-03-31 | 2010-12-17 | 글락소 그룹 리미티드 | 약물 융합체 및 컨주게이트 |
| CN102089325A (zh) | 2008-04-17 | 2011-06-08 | 埃博灵克斯股份有限公司 | 能够结合血清白蛋白的肽，以及包含其的化合物、构建体和多肽 |
| JP2012506237A (ja) * | 2008-10-21 | 2012-03-15 | ドマンティス リミテッド | Ｄｃ−ｓｉｇｎに対する結合特異性をもつリガンド |
| WO2010046357A1 (en) | 2008-10-21 | 2010-04-29 | Novo Nordisk A/S | Amylin derivatives |
| CA2743177A1 (en) * | 2008-11-24 | 2010-05-27 | Aileron Therapeutics, Inc. | Peptidomimetic macrocycles with improved properties |
| KR101498668B1 (ko) * | 2008-12-04 | 2015-03-06 | 한국생명공학연구원 | 고분비성 단백질의 스크리닝 및 재조합 단백질의 생산을 위한 융합 파트너로서 그의 용도 |
| WO2010063818A2 (en) | 2008-12-05 | 2010-06-10 | Glaxo Group Limited | Methods for selecting protease resistant polypeptides |
| MX2011008752A (es) | 2009-02-19 | 2011-09-06 | Glaxo Group Ltd | Variantes de union a anti-albumina de suero mejoradas. |
| ES2655071T3 (es) | 2009-02-19 | 2018-02-16 | Glaxo Group Limited | Variantes de unión de anti-albúmina de suero mejoradas |
| PE20120514A1 (es) | 2009-03-27 | 2012-05-14 | Glaxo Group Ltd | Fusiones y conjugados de agentes insulinotropicos o farmacos incretina con anticuerpos dab anti-albumina serica |
| US20120058116A1 (en) | 2009-04-24 | 2012-03-08 | Andrew Beaton | Fgfr1c antibody combinations |
| JP2012526080A (ja) * | 2009-05-06 | 2012-10-25 | ノバルティス アーゲー | 抗ＩＬ１−β抗体の併用療法 |
| EP2454285A2 (en) * | 2009-07-16 | 2012-05-23 | Glaxo Group Limited | Improved anti-serum albumin binding single variable domains |
| SG10201406063XA (en) * | 2009-09-30 | 2014-11-27 | Glaxo Group Ltd | Drug fusions and conjugates with extended half life |
| EP2509997B1 (en) * | 2009-12-07 | 2017-08-30 | i2 Pharmaceuticals, Inc. | Conjugates comprising an antibody surrogate scaffold with improved pharmacokinetic properties |
| CN102781959A (zh) | 2010-02-05 | 2012-11-14 | 埃博灵克斯股份有限公司 | 能够结合血清白蛋白的肽和包含所述肽的化合物、构建体和多肽 |
| JP2013528362A (ja) | 2010-04-21 | 2013-07-11 | グラクソ グループ リミテッド | 結合ドメイン |
| EA201291009A1 (ru) | 2010-05-20 | 2013-05-30 | Глаксо Груп Лимитед | Улучшенные связывающие варианты против сывороточного альбумина |
| NZ604805A (en) * | 2010-07-09 | 2014-09-26 | Affibody Ab | Polypeptides |
| US9012609B2 (en) | 2010-08-13 | 2015-04-21 | Glaxosmithkline Intellectual Property Development Limited | Anti-serum albumin binding variants |
| SG188204A1 (en) | 2010-08-20 | 2013-04-30 | Glaxo Group Ltd | Improved anti-serum albumin binding variants |
| JP2014502252A (ja) | 2010-09-28 | 2014-01-30 | アミリン・ファーマシューティカルズ，リミテッド・ライアビリティ・カンパニー | 作用持続時間が増した改変ポリペプチド |
| WO2012072731A2 (en) | 2010-12-01 | 2012-06-07 | Glaxo Group Limited | Improved anti-serum albumin binding single variable domains |
| WO2012104227A1 (en) | 2011-02-02 | 2012-08-09 | Glaxo Group Limited | Novel antigen binding proteins |
| WO2012136790A1 (en) | 2011-04-07 | 2012-10-11 | Glaxo Group Limited | Compositions comprising fusion proteins or conjugates with an improved half -life |
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