JP5025482B2 - 抗体製剤 - Google Patents
抗体製剤 Download PDFInfo
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- JP5025482B2 JP5025482B2 JP2007537982A JP2007537982A JP5025482B2 JP 5025482 B2 JP5025482 B2 JP 5025482B2 JP 2007537982 A JP2007537982 A JP 2007537982A JP 2007537982 A JP2007537982 A JP 2007537982A JP 5025482 B2 JP5025482 B2 JP 5025482B2
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Description
本発明は、ヒスチジン−酢酸緩衝液中で処方されたモノクローナル抗体、ならびにHER2のドメインIIに結合する抗体(例えば、パーツズマブ)を含む製剤およびDR5に結合する抗体(例えば、Apomab)を含む製剤を含めた抗体製剤に関するものである。
過去10年間に、バイオテクノロジーにおける進歩は、リコンビナントDNA技法を用いて薬学的応用のための多様なタンパク質を生産することを可能にした。タンパク質が伝統的な有機薬物および無機薬物よりも大型で複雑な(すなわち、複雑な三次元構造に加えて多数の官能基を有する)ことから、当該タンパク質の製剤は特別な問題を提起する。タンパク質が生物学的に活性のままであるためには、そのタンパク質のアミノ酸の少なくともコア配列のコンフォメーション完全性がインタクトな状態を保つ一方で、同時にそのタンパク質の多数の官能基を分解から保護しなければならない。タンパク質の分解経路は、化学的不安定性(すなわち新しい化学的実体を生じる、結合形成または開裂によるタンパク質の改変を伴う任意の過程)または物理的不安定性(すなわちタンパク質の高次構造の変化)を伴うことがある。化学的不安定性は、脱アミド、ラセミ化、加水分解、酸化、β−脱離またはジスルフィド交換に起因することがある。物理的不安定性は、例えば変性、凝集、沈殿または吸着に起因することがある。三つの最もよくみられるタンパク質分解経路は、タンパク質凝集、脱アミドおよび酸化である。Clelandら、Critical Reviews in Therapeutic Drug Carrier Systems 10(4): 307-377 (1993)。
薬学的応用に使用されるタンパク質には抗体が含まれる。治療に有用な抗体の例は、パーツズマブなどのHER2抗原に結合する抗体である。
HERファミリーのレセプターチロシンキナーゼは、細胞の成長、分化、および生存の重要な仲介物質である。このレセプターファミリーには、上皮成長因子レセプター(EGFR、BrbB1、またはHER1)、HER2(ErbB2またはp185neu)、HER3(ErbB3)、およびHER4(ErbB4またはtyro2)を含めた四つの異なるメンバーがある。
腫瘍壊死因子(TNF)スーパーファミリーに属する様々なリガンドおよびレセプターが当技術分野で同定された。当該リガンドには、腫瘍壊死因子−α(「TNF−α」)、腫瘍壊死因子−β(「TNF−β」または「リンホトキシン−α」)、リンホトキシン−β(「LT−β」)、CD30リガンド、CD27リガンド、CD40リガンド、OX−40リガンド、4−1BBリガンド、LIGHT、Apo−1リガンド(FasリガンドまたはCD95リガンドとも呼ばれる)、Apo−2リガンド(Apo2LまたはTRAILとも呼ばれる)、Apo−3リガンド(TWEAKとも呼ばれる)、APRIL、OPGリガンド(RANKリガンド、ODF、またはTRANCEとも呼ばれる)、およびTALL−I(BlyS、BAFFまたはTHANKとも呼ばれる)がある(例えば、Ashkenazi, Nature Review, 2:420-430 (2002); Ashkenazi and Dixit, Science, 281:1305-1308 (1998); Ashkenazi and Dixit, Curr. Opin. Cell Biol., 11:255-260 (2000); Golstein, Curr. Biol., 7:750-753 (1997); Wallach, Cytokine Reference, Academic Press, 2000, pages 377-411; Locksley et al., Cell, 104:487-501 (2001); Gruss and Dower, Blood, 85:3378-3404 (1995); Schmid et al., Proc. Natl. Acad. Sci., 83:1881 (1986); Dealtry et al., Eur. J. Immunol., 17:689 (1987); Pitti et al., J. Biol. Chem., 271:12687-12690 (1996); Wiley et al., Immunity, 3:673-682 (1995); Browning et al., Cell, 72:847-856 (1993); Armitage et al. Nature, 357:80-82 (1992);1997年1月16日に公開されたWO97/01633;1997年7月17日に公開されたWO97/25428; Marsters et al., Curr. Biol., 8:525-528 (1998); Chicheportiche et al., Biol. Chem., 272:32401-32410 (1997); Hahne et al., J. Exp. Med., 188:1185-1190 (1998); 1998年7月2日に公開されたWO98/28426;1998年10月22日に公開されたWO98/46751;1998年5月7日に公開されたWO/98/18921; Moore et al., Science, 285:260-263 (1999); Shu et al., J. Leukocyte Biol., 65:680 (1999); Schneider et al., J. Exp. Med., 189:1747-1756 (1999); Mukhopadhyay et al., J. Biol. Chem., 274:15978-15981 (1999)を参照されたい)。
本明細書における本発明は、少なくとも部分的に、モノクローナル抗体、特に脱アミドおよび/または凝集に感受性の全長IgG1抗体を処方するために特に有用な緩衝液としてのヒスチジン−酢酸(pH5.5から6.5)の同定に関するものである。その製剤は、その中の抗体産物の分解を遅延させる。
I.定義
用語「薬学的製剤」は、活性成分の生物学的活性を有効にさせる形態の調製物であって、その製剤が投与されるであろう対象に許容されず有毒である追加の構成要素を含有しない調製物を指す。当該製剤は無菌である。
CDR L1配列RASSSVSYXH(配列中、XはMまたはL(配列番号67)、例えば配列番号57(図18A))、
CDR L2配列(配列番号58(図18A))、
CDR L3配列QQWXFNPPT(配列中、XはSまたはA(配列番号68)、例えば配列番号59(図18A))、
CDR H1配列(配列番号60(図18B))、
CDR H2配列AIYPGNGXTSYNQKFKG(配列中、XはDまたはA(配列番号69)、例えば配列番号61(図18B))、および
CDR H3配列VVYYSXXYWYFDV(配列中、位置6のXはN、A、Y、WまたはDであり、位置7のXはSまたはRである(配列番号70)、例えば配列番号62(図18B))。
本発明により処方できる抗体を産生するための技法は、以下の通りである。
好ましくは、その抗体が結合する抗原は、生物学的に重要な糖タンパク質であり、疾患または障害を患う哺乳動物へのその抗体の投与は、その哺乳動物に治療上の利益を生じることができる。しかし、非ポリペプチド抗原に対する抗体(腫瘍関連糖脂質抗原など、米国特許第5,091,178号参照)も考えられている。
モノクローナル抗体は、実質的に均一な抗体の集団から得られ、すなわち、その集団を含む個別の抗体は、モノクローナル抗体の産生中に生じうる可能性のある変異体を除いて、同一であり、かつ/または同じエピトープと結合する。このように、修飾語「モノクローナル」は、別個の抗体の混合物ではない抗体の性質を意味する。
非ヒト抗体をヒト化するための方法は、当技術分野に記載されている。好ましくは、ヒト化抗体は、非ヒトである起源からその抗体に導入された一つまたは複数のアミノ酸残基を有する。これらの非ヒトアミノ酸残基は、しばしば、「輸入(import)」残基と称される。この残基は、典型的には「輸入」可変ドメインから取り入れられる。ヒト化は、ヒト抗体の対応配列の代わりに超可変部配列に置換することによって、Winterおよび共同研究者らの方法(Jones et al., Nature, 321:522-525 (1986); Riechmann et al., Nature, 332:323-327 (1988); Verhoeyen et al., Science, 239:1534-1536 (1988))に従って本質的に行うことができる。従って、当該「ヒト化」抗体は、インタクトなヒト可変ドメインよりも実質的に小さな配列が非ヒト種由来の対応する配列に置換されているキメラ抗体(米国特許第4,816,567号)である。実際には、ヒト化抗体は、典型的には、一部の超可変部残基と、可能性があることには一部のFR残基とが、げっ歯動物抗体の類似部位に由来する残基に置換されているヒト抗体である。
ヒト化の代替として、ヒト抗体を発生させることができる。例えば、免疫処置した際に、内因性免疫グロブリン産生の不在下でヒト抗体の全レパートリーを産生できるトランスジェニック動物(例えば、マウス)を作製することが今や可能である。例えば、キメラおよび生殖細胞系突然変異マウスにおける抗体重鎖結合部(JH)遺伝子の同型接合型欠失は、内因性抗体産生の完全な阻害を招くことが記載されている。当該生殖細胞系突然変異マウスにヒト生殖細胞系免疫グロブリン遺伝子アレイを導入する結果として、抗原による攻撃の際にヒト抗体の産生が生じるものである。例えば、Jakobovits et al., Proc. Natl. Acad. Sci. USA, 90:2551 (1993); Jakobovits et al., Nature, 362:255-258 (1993); Bruggermann et al., Year in Immuno., 7:33 (1993);ならびに米国特許第5,591,669号、第5,589,369号および第5,545,807号を参照されたい。
種々の技法が抗体フラグメントの産生のために開発されてきた。伝統的には、これらのフラグメントは、全長抗体のタンパク質分解消化を介して誘導された(例えば、Morimoto et al., Journal of Biochemical and Biophysical Methods 24: 107-117 (1992);およびBrennan et al., Science, 229:81 (1985)を参照されたい)。しかし、これらのフラグメントを、今や組換え宿主細胞によって直接産生することができる。例えば、その抗体フラグメントを、上記の抗体ファージライブラリーから単離することができる。または、Fab’−SHフラグメントを、E.coliから直接回収して、化学的に結合させてF(ab’)2フラグメントを形成させることができる(Carter et al., Bio/Technology 10:163-167 (1992))。別のアプローチにより、F(ab’)2フラグメントを、組換え宿主細胞培養物から直接単離することができる。抗体フラグメントの産生のためのその他の技法は、当業者に明白であろう。他の態様では、選択した抗体は一本鎖Fvフラグメント(scFv)である。WO93/16185;米国特許第5,571,894号;および第5,587,458号を参照されたい。この抗体フラグメントは、例えば、米国特許第5,641,870号に例えば記載される通り「線状抗体」(linear antibody)でもありうる。当該線状抗体フラグメントは、単一特異性または二重特異性でありうる。
二重特異性抗体は、少なくとも2つの異なるエピトープに対して結合特異性を有する抗体である。例示的な二重特異性抗体は、HER2タンパク質の2つの異なるエピトープに結合することができる。その他の当該抗体は、HER2結合部位と、EGFR、HER3および/またはHER4に対する結合部位とを組み合わせることができる。または、細胞防御メカニズムをHER2発現細胞に集中させるために、T細胞レセプター分子(例えば、CD2もしくはCD3)のような、またはFcγRI(CD64)、FcγRII(CD32)、およびFcγRIII(CD16)などの、IgGに対するFcレセプター(FcγR)のような、白血球上のトリガー分子に結合するアームとHER2アームを組み合わせることができる。HER2を発現する細胞に細胞毒性薬を局在化させるために、二重特異性抗体を使用することもできる。これらの抗体は、HER2結合アームと、細胞毒性薬(例えば、サポリン、抗インターフェロン−α、ビンカアルカロイド、リシン(ricin)A鎖、メトトレキサート、または放射性同位体ハプテン)と結合するアームとを有する。二重特異性抗体を、全長抗体または抗体フラグメント(例えば、F(ab’)2二重特異性抗体)として調製することができる。
本明細書に記載された抗体のアミノ酸配列の改変が考えられている。例えば、抗体の結合親和性および/または他の生物学的性質を改善することが望ましいことがある。適切なヌクレオチド変化を抗体の核酸に導入することにより、またはペプチド合成により、抗体のアミノ酸配列変異体を調製する。当該改変には、例えば、抗体のアミノ酸配列内の残基の欠失および/または挿入および/または置換がある。欠失、挿入、および置換の任意の組み合わせは、最終構築物に達するように作製されるが、ただし、その最終構築物は所望の性質を有する。そのアミノ酸変化は、グリコシル化部位の数または位置を変化させるように、抗体の翻訳後プロセスを変更することもできる。
(1)非極性:Ala(A)、Val(V)、Leu(L)、Ile(I)、Pro(P)、Phe(F)、Trp(W)、Met(M)
(2)非荷電極性:Gly(G)、Ser(S)、Thr(T)、Cys(C)、Tyr(Y)、Asn(N)、Gln(Q)
(3)酸性:Asp(D)、Glu(E)
(4)塩基性:Lys(K)、Arg(R)、His(H)。
(1)疎水性:ノルロイシン、Met、Ala、Val、Leu、Ile;
(2)中性親水性:Cys、Ser、Thr、Asn、Gln;
(3)酸性:Asp、Glu;
(4)塩基性:His、Lys、Arg;
(5)鎖配向に影響する残基:Gly、Pro;
(6)芳香族:Trp、Tyr、Phe。
抗体を発生させる技法は上述されている。所望により、ある生物学的特性を有する抗体をさらに選択することができる。
本発明は、化学療法剤、毒素(例えば、細菌、真菌、植物または動物起源の小分子毒素または酵素活性毒素であって、そのフラグメントおよび/または変異体を含む)、または放射性同位体(すなわち、放射性コンジュゲート)などの細胞毒性薬にコンジュゲーションした抗体を含む免疫コンジュゲートにも関するものである。
抗体のその他の改変が本明細書において考えられている。例えば、多様な非タンパク質性ポリマー、例えば、ポリエチレングリコール、ポリプロピレングリコール、ポリオキシアルキレン、またはポリエチレングリコールとポリプロピレングリコールとのコポリマーのうちの一つに抗体を連結することができる。例えばコアセルベーション技法もしくは界面重合によって調製されたマイクロカプセル(例えば、それぞれヒドロキシメチルセルロースマイクロカプセルまたはゼラチンマイクロカプセルおよびポリメタクリル酸メチルマイクロカプセル)に、コロイド状薬物送達系(例えば、リポソーム、アルブミンミクロスフェア、ミクロエマルション、ナノ粒子、およびナノカプセル)に、またはマクロエマルションに、抗体を捕捉することもできる。このような技法は、Remington's Pharmaceutical Sciences, 16th edition, Oslo, A., Ed., (1980)に開示されている。
本発明により処方できる抗体の例には以下のものがあるが、それに限定されるわけではない:
抗ErbB抗体、本明細書にさらに詳細に記載された抗体などの抗HER2抗体を含む;
B細胞表面マーカーに結合する抗体、CD19、CD20(例えば、リツキシマブ(RITUXAN(登録商標))およびヒト化2H7)、CD22、CD40またはBR3など;
IgEに結合する抗体、ジェネンテックから市販されているオマリズマブ(XOLAIR(登録商標))、E26(本明細書の図17A〜B)、HAE1(本明細書の図17A〜B)、Fc部の位置265にアミノ酸置換を有する抗IgE抗体(US2004/0191244A1)、Hu−901(本明細書の図17A〜B)、WO2004/070011におけるような抗IgE抗体、またはこれら抗IgE抗体のうち任意のものの可変ドメインを含む抗体(抗体フラグメントおよび全長抗体を含む)。Prestaら、J. Immunol. 151:2623-2632 (1993);国際公開WO95/19181;1998年2月3日に発行された米国特許第5,714,338号;1992年2月25日に発行された米国特許第5,091,313号;1993年3月4日に公開されたWO93/04173;1999年1月14日に公開されたWO99/01556;および米国特許第5,714,338号も参照されたい;
血管内皮成長因子(VEGF)またはそのレセプターに結合する抗体、ジェネンテックから市販されているベバシズマブ(AVASTIN(商標))およびラニビズマブ(LUCENTIS(商標))を含む;
抗IL−8抗体(St John et al., Chest, 103:932 (1993)および国際公開WO95/23865);
抗PSCA抗体(WO01/40309);
抗CD40抗体、S2C6およびそのヒト化変異体を含む(WO00/75348);
抗CD11a抗体、エファリズマブ(RAPTIVA(登録商標))を含む(米国特許第5,622,700号、WO98/23761、Steppe et al., Transplant Intl. 4:3-7 (1991)、およびHourmant et al., Transplantation 58:377-380 (1994));
抗CD18抗体(1997年4月22日に発行された米国特許第5,622,700号または1997年7月31日に公開されたWO97/26912の通り);
抗Apo−2レセプター抗体(1998年11月19日に公開されたWO98/51793);
抗TNF−α抗体、cA2(REMICADE(登録商標))、CDP571およびMAK−195を含む(1997年9月30日に発行された米国特許第5,672,347号、Lorenz et al. J. Immunol. 156(4):1646-1653 (1996)、およびDhainaut et al. Crit. Care Med. 23(9):1461-1469 (1995)参照);
抗組織因子(TF)(1994年11月9日に付与された欧州特許第0420937B1);
抗ヒトα4β7インテグリン(1998年2月19日に公開されたWO98/06248);
抗EGFR抗体、1996年12月19日に公開されたWO96/40210におけるようなキメラ化またはヒト化225抗体を含む;
抗CD3抗体、OKT3など(1985年5月7日に発行された米国特許第4,515,893号);
抗CD25抗体または抗tac抗体、CHI−621(SIMULECT(登録商標))および(ZENAPAX(登録商標))など(1997年12月2日に発行された米国特許第5,693,762号参照);
抗CD4抗体、cM−7412抗体など(Choy et al. Arthritis Rheum 39(1):52-56 (1996));
抗CD52抗体、CAMPATH−1Hなど(Riechmann et al. Nature 332:323-337 (1988));
抗Fcレセプター抗体、Grazianoら、J. Immunol. 155(10):4996-5002 (1995)におけるようなFcγRIに対するM22抗体など;
抗ガン胎児抗原(CEA)抗体、hMN−14など(Sharkey et al. Cancer Res. 55(23 Suppl): 5935s-5945s (1995);
huBrE−3、hu−Mc3およびCHL6を含めた乳房上皮細胞に対する抗体(Ceriani et al. Cancer Res. 55(23): 5852s-5856s (1995);およびRichman et al. Cancer Res. 55(23 Supp): 5916s-5920s (1995));
C242などの結腸ガン細胞に結合する抗体(Litton et al. Eur J. Immunol. 26(1): 1-9 (1996));
抗CD38抗体、例えばAT13/5(Ellis et al. J. Immunol. 155(2):925-937 (1995));
抗CD33抗体、Hu M195など(Jurcic et al. Cancer Res 55(23 Suppl):5908s-5910s (1995)およびCMA−676またはCDP771);
抗CD22抗体、LL2またはLymphoCideなど(Juweid et al. Cancer Res 55(23 Suppl):5899s-5907s (1995);
抗EpCAM抗体、17−1A(PANOREX(登録商標))など;
抗GpIIb/IIIa抗体、アブシキシマブすなわちc7E3 Fab(REOPRO(登録商標))など;
抗RSV抗体、MEDI−493(SYNAGIS(登録商標))など;
抗CMV抗体、PROTOVIR(登録商標)など;
抗HIV抗体、PRO542など;
抗肝炎抗体、抗Hep B抗体OSTAVIR(登録商標)など;
抗CA125抗体OvaRex;
抗イディオタイプGD3エピトープ抗体BEC2;
抗αvβ3抗体VITAXIN(登録商標);
抗ヒト腎細胞ガン抗体、ch−G250、ING−1など;
抗ヒト17−1A抗体(3622W94);
抗ヒト結腸直腸腫瘍抗体(A33);
GD3ガングリオシドに対する抗ヒト黒色腫抗体R24;
抗ヒト扁平上皮細胞ガン(SF−25);ならびに
抗ヒト白血球抗原(HLA)抗体、Smart ID10および抗HLA DR抗体Oncolym(Lym−1)など。
本発明は、少なくとも一局面では、主要種抗体とその一つまたは複数の変異体との混合物を含む組成物を含む製剤に関するものである。その主要種抗体がHER2と結合する場合、好ましくはそのHER2抗体(主要種HER2抗体およびその抗体変異体の一方または両方)は、HER2のドメインIIに結合し、トラスツズマブよりも効果的にHERの二量体化を阻害し、かつ/またはHER2のヘテロ二量体結合部位に結合する抗体である。その主要種抗体の本明細書における好ましい態様は、配列番号3および4の可変軽鎖および可変重鎖アミノ酸配列を含む抗体であり、最も好ましくは配列番号15および23より選択される軽鎖アミノ酸配列と、配列番号16および24より選択される重鎖アミノ酸配列とを含む抗体である。
本発明は、第1の局面では、ヒスチジン−酢酸緩衝液(pH5.5から6.5、好ましくはpH5.8から6.2)中にモノクローナル抗体、好ましくは全長ヒトまたはヒト化IgG1抗体を含む安定な薬学的製剤を提供する。しかし、その製剤中の抗体は、FabまたはF(ab’)2フラグメントなどの、抗原結合領域を含む抗体フラグメントでありうる。
一態様において、本発明は対象における疾患または障害を処置する方法を提供し、その方法は、本明細書に記載された製剤を、その疾患または障害を処置するのに有効な量で対象に投与することを含む。
本発明の別の態様では、本発明の薬学的製剤を含有し、その使用説明書を提供する製品が提供される。その製品は容器を備える。適切な容器には、例えば、ボトル、バイアル(例えば2チャンバーバイアル)、注射器(2チャンバー注射器など)および試験管がある。その容器は、ガラスまたはプラスチックなどの多様な材料から形成されうる。その容器はその製剤を収容し、その容器の上、またはその容器に付随するラベルは、使用方法を表示すことができる。その製剤を収容している容器は、再構成された製剤の反復投与(例えば2〜6回の投与)を見込んだ多使用バイアルでありうる。その製品は、他の緩衝液、希釈剤、フィルター、針、注射器、および前節で言及したような使用説明書を有する添付文書を含めた、商業的観点およびユーザーの観点から望ましい他の材料をさらに含むことがある。
安定なパーツズマブ液体製剤
これらの実施例は、約10mg/mL〜180mg/mLのタンパク質濃度範囲でパーツズマブを含む安定な液体製剤の開発および安定性検査について記載する。選択された製剤は低い濁度を有し、物理的および化学的に安定であった。腐食のリスクを減らすためにその製剤から塩化物イオンを除去した。その製剤は等張で、皮下または筋肉内デリバリーに適していた。撹拌ストレス時の不溶性凝集物の形成は、ポリソルベート20を入れる必要なしにヒスチジン−酢酸およびスクロースの製剤を用いて防止された。
色、外観および透明度(CAC)
試料の色、外観、および透明度は、室温で蛍光灯下で白色および黒色背景に対してバイアルを肉眼検査することによって決定した。
一定分量の液体製品を最初に製剤緩衝液で希釈して、278nm付近のAmaxが0.5〜1.0吸光度単位に収まるようにした。光路長1cmの水晶セル中で、希釈した試料のUV吸光度をHP8453分光光度計で測定した。吸光度を278nmおよび320nmで測定した。320nmの吸光度を使用して、大きな凝集物、泡および粒子が原因のバックグラウンド光散乱を補正する。これらの測定値について製剤緩衝液をブランク試料として使用した。吸光率1.50(mg/mL)-1cm-1を用いてタンパク質濃度を決定した。
RADIOMETER COPENHAGEN PHM82(商標)pHメータを用いて室温でpHを測定した。使用したプローブは、放射計コネクター(Sigma, Cat#E-5759)を有するガラス/参照複合電極であった。pHメータのキャリブレーションにpH4.01およびpH7.00の標準溶液(EM Science)を使用した。
陽イオン交換クロマトグラフィーを採用して電荷変異体における変化を測定した。このアッセイは、HP1100(商標)HPLCシステムでDIONEX PROPAC WCX−10(商標)カラムを利用する。pH6.0の20mM MESを含有する移動相Aで試料を1mg/mLに希釈した。次に、希釈された試料50mLを、常温に保ったカラムにロードした。20mM MES、250mM NaCl(pH6.0)を含有する移動相Bを用いた緩いNaCl勾配でピークを溶出した。溶出液を280nmでモニターした。HP CHEMSTATION(商標)ソフトウェア(Rev A08.03)を用いてデータを分析した。
FabおよびF(ab’)2フラグメントの純度をCZEによって決定した。このアッセイを、BIOCAP XL(商標)キャピラリー、内径50μm、全長44.6cmおよび検出器まで40cmのBIORAD BIOFOCUS(商標)3000(商標)キャピラリー電気泳動システムで行った。
サイズ排除クロマトグラフィーを使用して凝集物およびフラグメントを定量した。このアッセイは、TSK G3000SWXL(商標)、7.8×300mmカラムを利用し、HP1100(商標)HPLCシステムで行う。移動相で試料を10mg/mLに希釈し、インジェクション容積は20μLであった。その移動相は、pH6.8の100mM K2HPO4であり、タンパク質を0.5mL/minのアイソクラチックな勾配で45分間溶出した。溶出液の吸光度を280nmでモニターした。HP CHEMSTATION(商標)ソフトウェア(Rev A08.03)を用いて積分を行った。
パーツズマブがヒト乳ガン細胞系MDA−MB−175−VIIの増殖を阻害する能力を測定することによって、パーツズマブの生物学的活性を決定した。
パーツズマブのFabおよびF(ab’)2抗体フラグメントを以下の緩衝液条件でタンパク質濃度1.0mg/mLで製剤した:
10mMクエン酸、140mM NaCl、pH4.0;
10mMコハク酸、140mM NaCl、pH5.0;
10mMコハク酸、140mM NaCl、pH6.0;
10mMヒスチジン、140mM NaCl、pH7.0;および
10mMグリシルグリシン、140mM NaCl、pH8.0。
パーツズマブを、120mMスクロースおよび0.02%ポリソルベート20を有する20mMヒスチジン−酢酸緩衝液中で製剤した。酢酸を用いて5.0から7.0の間の最終pHに製剤のpHを調整した。タンパク質濃度は30mg/mLであった。各製剤を3ccUSPタイプIガラスバイアルに充填し、安定性分析のために40℃で保存した。結果は、パーツズマブがpH6.0付近で最も安定であったことを示した。
タンパク質濃度100mg/mLのパーツズマブ製剤を以下の賦形剤中で調製した:
(1)10mMヒスチジン−HCl、240mMスクロース、0.02%ポリソルベート20、pH6.0;
(2)10mMヒスチジン−酢酸、240mMスクロース、0.02%ポリソルベート20、pH6.0;
(3)10mMヒスチジン−リン酸、240mMスクロース、0.02%ポリソルベート20、pH6.0;
(4)10mMヒスチジン−硫酸、240mMスクロース、0.02%ポリソルベート20、pH6.0。
パーツズマブを、以下の緩衝液中で限外濾過/ダイアフィルトレーションにより様々な濃度に濃縮した:
(1)20mMヒスチジン−酢酸、pH6.0;
(2)10mMヒスチジン−HCl、pH6.0、および
(3)10mM ヒスチジン−硫酸、pH6.0.
パーツズマブを、20mMヒスチジン−酢酸、120mMスクロース、0.02%ポリソルベート20(pH6.0)中に30mg/mLで処方した。パーツズマブを、316LおよびHASTELLOY(商標)のステンレススチールミニチュアタンクに充填した。全ての試料を−20℃および5℃で保存し、質(CAC)、純度(SEC、IEC)および強度(UV−Vis)について評価した。安定性分析は、パーツズマブが−20℃および5℃で少なくとも3か月間保存時にこの製剤中で安定であったことを示した。無塩化物製剤は、316LおよびHASTELLOY(商標)のステンレススチールタンクと適合性である。
パーツズマブをタンジェンシャルフロー濾過(TFF)を用いて処方した。最終製剤は、タンパク質濃度30mg/mLで20mMヒスチジン−酢酸、120mMスクロース、0.02%ポリソルベート20(pH6.0)を含有する。試料を、20mm FLUROTEC(商標)表面のブチルゴム栓でキャップした20Ml FORMA VITRUM(商標)USPタイプIガラスバイアルに充填し、アルミニウム押し上げ式キャップで密封した。全ての試料を−70℃、5℃、15℃で保存し、質(CAC)、純度(SEC、IEC)、強度(UV−Vis)、および効力(バイオアッセイ)について安定性を評価した。結果は、5℃および15℃で少なくとも3か月間保存したときにこの製剤中のパーツズマブが安定であることを示した。
以下の緩衝液条件でパーツズマブを100mg/mLで処方した:
(1)10mMヒスチジン−HCl、pH6.0;
(2)10mMヒスチジン−HCl、240mMスクロース、pH6.0;
(3)20mMコハク酸、pH6.0;および
(4)20mMコハク酸、240mMスクロース、pH6.0。
以下の製剤中でパーツズマブを調製した:
(1)25mg/mLパーツズマブ、10mMヒスチジン−HCl、240mMスクロース、pH6.0;
(2)50mg/mLパーツズマブ、10mMヒスチジン−HCl、240mMスクロース、pH6.0;
(3)60mg/mLパーツズマブ、20mMヒスチジン−酢酸、120mMスクロース、pH6.0。
パーツズマブを以下のように処方した:
(1)100mg/mLタンパク質、10mMヒスチジン−HCl、pH6.0;
(2)100mg/mLタンパク質、20mMコハク酸、pH6.0;
(3)60mg/mLタンパク質、20mMヒスチジン−酢酸、pH6.0。
治療的使用のための好ましいパーツズマブ製剤は、本質的に20mMヒスチジン酢酸、120mMスクロース、0.02%ポリソルベート20(pH6.0)中の30mg/mLパーツズマブからなる。
バイアル:20cc公定VitrumタイプIガラス
栓:20mm DAIKYO GREY(商標)、フッ素樹脂ラミネート
キャップ:20mm押し上げ式アルミニウム
充填体積:14.50mL
デリバリー:生理食塩水IVバッグにパーツズマブ14.0mL。
バイアル:50cc公定VitrumタイプIガラス
栓:20mm DAIKYO GREY(商標)、フッ素樹脂ラミネート
キャップ:20mm押し上げ式アルミニウム
充填体積:36.0mL
デリバリー:生理食塩水IVバッグにパーツズマブ35.0mL。
本実施例は、第I相および第II相臨床試験で使用された別のパーツズマブ製剤に関するものである。この組成物は、25mg/mlパーツズマブ、10mMヒスチジン−HCl緩衝液、240mMスクロース、0.02%ポリソルベート20、pH6.0からなる。
細胞のアポトーシスは、内因性および外因性経路に仲介される。化学療法は、細胞の損傷を引き起こすことがあり、細胞の損傷に応答して内因性経路によりアポトーシスを誘発しうる。しかし、ガン細胞はしばしばp53腫瘍抑制遺伝子の突然変異により化学療法に対する耐性を発生する(Ashkenazi A. Targeting Death and Decoy Receptors of the Tumour-Necrosis Factor Superfamily. Nature Reviews 2:420-430 (2002))。細胞表面に局在するDR4およびDR5などのデスレセプターは、p53を伴わない外因性経路を介してアポトーシスを誘発する。Apo2Lなどのアゴニスト分子はDR4およびDR5レセプターに結合し、Fas関連デスドメインを介してカスパーゼ8および10を活性化する。次に、カスパーゼ8および10は、カスパーゼ3、6および7を活性化してアポトーシスを誘導する。腫瘍細胞上のデスレセプターの分子シグナル伝達は、通常の治療に耐性のガン細胞の除去に治療的潜在性を有し、Apo2Lのような分子は現在臨床的評価の途中である。
リコンビナント産生されたApomabは、非常に希薄なタンパク質濃度および高pHを有した。MILLIPORE PELLICON(商標)XL、PLCGC10、50cm膜を用いたMillipore実験室規模タンジェンシャルフロー濾過(TFF)システムを用いてその材料を約20mg/mLまで濃縮し、交換して20mM酢酸ナトリウム(pH5.0)緩衝液中になるようにした。トレハロースおよびTWEEN20(登録商標)を有しない酢酸ナトリウム、ヒスチジン酢酸塩、およびリン酸ナトリウムを用いて、10000Da分子量カットオフ膜(Pierce, Inc)を用いた透析を使用して、4.0から7.0のpH範囲にわたる様々な緩衝系中でApomab試料を処方した。最終透析に240mMのトレハロースを添加した。透析後に、0.02%TWEEN20(商標)をその製剤に添加して、試料を0.22μmフィルター(Millipore, Inc.)で濾過した。Apomabの容積0.5mLを無菌3ccガラスバイアル(Forma Vitrum, Inc.)中に充填し、13mm栓(Daikyo, Inc)で密封した。タンパク質の安定性を−70℃、5℃、30℃、および40℃で最長3か月間保存して評価した。
薬物産物の安定性を検査するために、5cc FORMA VITRUM(登録商標)ガラスバイアル中に充填されたApomab処方原体を処方した。処方された抗体5.5mLをバイアルに充填し、20mm DAIKYO(登録商標)栓を取付け、−70℃、5℃、30℃、および40℃で直立させて保存した。
試料の透明度、外観、および色を、黒および白色背景を有する光検査場所を使用して蛍光灯下で肉眼評定した。原薬の分析のために、ミニタンクの試料を検査用の3ccガラスバイアルに移した。
緩衝液の測定のためにTHERMO ORION SURE−FLOW ROSS(商標)セミミクロpH電極、またはタンパク質pHスクリーニング試料の測定のためにTHERMO ORION GLS(商標)複合マイクロpH電極、毒性学的安定性試料のためにBeckmanマイクロ電極プローブを用いて室温でpHを測定した。METERLAB(商標)pHM240pH/イオンメータ(Radiometer Analytical)をpH7およびpH4の標準緩衝液(EM Science)で毎日キャリブレーションした。
AGILENT8453(商標)分光光度計を用いた紫外吸収分光法によりタンパク質濃度を決定した。適切な製剤緩衝液ブランクで試料を希釈して0.5から1.0の吸光度にした。その装置について希釈溶液をブランクとして使用して、240から500nmまでスペクトルをスキャンした。279nmでの吸光度から320nmでの吸光度の値を引いて、オフセットおよび光散乱について補正した。タンパク質濃度を次式により計算した:
ダイオードアレイ検出器を備える1100シリーズHPLC(Agilent Technologies, Inc.)でイオン交換クロマトグラフィーを実施した。PROPAC WCX−1O(商標)(Dionex)カラム(4×250mm)で流速0.5mL/minでカラム温度40℃を用いてクロマトグラフィーを実施した。移動相Aは、25mMリン酸ナトリウム(pH6.5)であった。移動相Bは、移動相Aと同じ緩衝液中の100mM塩化ナトリウムであった。カラムを100%移動相Aで平衡化した。試料のpHスクリーニングのために、量20mgのApomabをカラムにロードし、吸光度を214nmでモニターした。以下の勾配でカラムからタンパク質を溶出させた:
ダイオードアレイ検出器を備える1100シリーズHPLC(Agilent Technologies, Inc.)でサイズ排除クロマトグラフィーを実施した。量50μgのApomabをTSK Gel3000SWXL(商標)(7.8×300mm)カラムにロードし、pHスクリーニング用試料について流速0.9mL/minで20分間、毒性学的安定性試料について0.5mL/minで30分間、移動相として0.20Mリン酸カリウム、0.25M塩化カリウム(pH6.2)を用いて運転した。吸光度を280nmでモニターした。
効力バイオアッセイの目的は、ALAMARBLUE(商標)を用いてApomabがColo205細胞を殺滅する能力を測定することであった。Colo205は結腸ガン細胞系であり、DR5およびDR4両方のデスレセプターを発現する。このアッセイは、代謝活性の検出に基づく蛍光測定/比色測定用成長指示薬を組み込んでいる。ALAMARBLUE(商標)は、酸化状態で青色で非蛍光性の酸化還元色素である。細胞内代謝性還元は、その色素を蛍光性でもある赤色色素に変換する。色および蛍光の変化は代謝活性および生存細胞数と比例する。細胞が死滅するとシグナルは減少した。抗Fcを有する媒質中でApomabを希釈し、次に、Colo205細胞をApomab試料に添加して37℃で48時間インキュベートした。ALAMARBLUE(商標)を最後の2〜3時間に添加する。平板を励起波長530nmおよび発光波長590nmで読み取り、相対蛍光単位(RFU)を得た。KALEIDAGRAPH(商標)によってデータを分析した。殺滅の希釈曲線を作製した。
製剤pHのスクリーニング研究
非増幅安定細胞系から産生されたApomabを用いて、抗体安定性に及ぼすpHの作用を検討した。この分析のために、pH4.0、4.5、5.0、5.5の20mM酢酸ナトリウム緩衝液;pH6.0および6.5の20mMヒスチジン酢酸塩緩衝液;およびpH7.0の20mMリン酸ナトリウム緩衝液中に20mg/mL抗体でApomabを処方した。これらの製剤の全ては、240mMトレハロースおよび0.02%TWEEN20(登録商標)を含有した。これらの製剤を温度−70℃、5℃、30℃、および40℃で最長3か月間保存し、タンパク質の安定性を、CAC、pH、濃度、SECおよびIECを含めた様々な分析アッセイにより決定した。試料の保存時にCAC、pHまたはタンパク質濃度に有意な変化は観察されなかった。
原薬についての凍結解凍安定性データを表8に示す。
Apomabについての製剤を選択するために製剤スクリーニング研究を行った。240mMトレハロース二水和物および0.02%ポリソルベート20を有する酢酸ナトリウム、ヒスチジン酢酸塩、およびリン酸ナトリウムを緩衝液として用いたpH範囲4.0から7.0にわたるpHスクリーニングは、ApomabがpH6.0の溶液中で最も安定であることを示した。したがって、20mMヒスチジン酢酸塩、240mMトレハロース、0.02%ポリソルベート2(pH6.0)からなる製剤が開発され、実験的に安定であることが実証された。この製剤を用いて、Apomabは5℃で少なくとも12か月間安定であることが示された。さらに、316Lステンレススチール容器中に保存されたときに、Apomabは−20℃で少なくとも12か月間および5℃で3か月間安定であることが示された。Apomabは3回の凍結/解凍サイクルに供されたときに安定であることも示された。
Claims (7)
- 20mg/mLから40mg/mLの濃度のパーツズマブ、10mMから40mMの濃度のヒスチジン−酢酸緩衝液、60mMから250mMの濃度のスクロース、ならびに0.01%から0.1%の濃度のポリソルベート20を含む、薬学的製剤であって、ここで該製剤のpHが5.5から6.5であり、パーツズマブがそれぞれ配列番号3および4として示される可変軽鎖および可変重鎖アミノ酸配列を含む、薬学的製剤。
- パーツズマブが、配列番号15として示される軽鎖アミノ酸配列と、配列番号16として示される重鎖アミノ酸配列とを含む、請求項1記載の製剤。
- 製剤のpHが5.8から6.2である、請求項1または2記載の製剤。
- 30mg/mLのパーツズマブ、20mMのヒスチジン−酢酸、120mMのスクロース、および0.02%のポリソルベート20を含み、pHが6.0である、請求項1から3のいずれか一項記載の薬学的製剤。
- 対象における疾患または傷害を処置する方法における使用のための請求項1から4のいずれか一項記載の薬学的製剤であって、該方法が該疾患または障害を処置するのに有効な量の該製剤を対象に投与する段階を含む、薬学的製剤。
- ガンの処置のための方法における使用のための請求項1から4のいずれか一項記載の薬学的製剤であって、該方法がガンを処置するのに有効な量の該製剤を対象に投与する段階を含む薬学的製剤。
- ガンがHER2発現ガンである、請求項6記載の薬学的製剤。
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