JP6328087B2 - 静電的ステアリング(electrostaticsteering)効果を用いた抗体Fcヘテロ二量体分子を作製するための方法 - Google Patents
静電的ステアリング(electrostaticsteering)効果を用いた抗体Fcヘテロ二量体分子を作製するための方法 Download PDFInfo
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- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
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- C07K16/468—Immunoglobulins having two or more different antigen binding sites, e.g. multifunctional antibodies
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- C07K2317/526—CH3 domain
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Description
び同僚らは、「ノブを穴に(knobs−into−holes)」戦略を用いて、ヘテロ二量体化のため、重鎖を操作した(Ridgway, Prestaら 1996; Atwell, Ridgwayら 1997; Merchant, Zhuら 1998; Carter 2001)。「ノブを穴に」概念は、元来、隣接するαらせん間のアミノ酸側鎖のパッキングのためのモデルとして、Crickによって提唱された(Crick 1952)。カーターおよび同僚らは、より小さいアミノ酸側鎖をより大きいもので置き換えることによって、第一の鎖のCH3ドメイン接合部分(interface)にノブを生成し(例えば、T366Y);そして、より大きいアミノ酸側鎖をより小さいもので置き換えることによって、第二の鎖のCH3接合部分の並置される位に穴を生成した(例えば、Y407T)。並置される位にノブおよび穴を生成するための基礎は、ノブおよび穴の相互作用がヘテロ二量体形成に有利であり、一方、ノブ−ノブおよび穴−穴相互作用が、それぞれ、立体衝突、および有利な相互作用の欠失のため、ホモ二量体形成を妨害することである。「ノブを穴に」突然変異はまた、ヘテロ二量体形成を増進するため、CH3ドメイン間ジスルフィド結合操作と組み合わされた(Sowdhamini, Srinivasanら 1989; Atwell, Ridgwayら 1997)。これらの突然変異に加えて、投入DNA比もまた、収量を最大にするために多様にされた(Merchant, Zhuら 1998)。「ノブを穴に」技術は、米国特許第5,731,168号および第7,183,076号に開示される。
、CH2=アミノ酸111〜220、CH3=221〜327)の定常領域を含む。当業者の間では、IgG分子の多様なドメインに対応する正確なアミノ酸の理解に相違がありうる。したがって、上記に要約するドメインのN末端またはC末端は、1、2、3、4、5、6、7、8、9アミノ酸、伸長または短縮され、または10アミノ酸さえ、伸長または短縮されうる。また、ドメインを指定するための本明細書に用いる番号付けスキームは、本特許出願の他の部分で用いるKabatのEU番号付けスキームとは異なる。例えば、IgG1「CH3=224〜330」は、EU番号付けスキームにおける「CH3=341〜447」に対応する。
−−Asp B 356’;図5)。
を増進することも可能である。
表2b:静電的ステアリング効果を増進するためのさらなる単一電荷残基突然変異a
各正電荷残基(LysおよびArg)を2つの負電荷残基(AspまたはGlu)に突然変異させてもよいし、そして逆も可能であり、そしてその結果、本明細書に記載する方法は、多くの組み合わせを提供する。本明細書において、突然変異部位を取り巻く残基および水分子の役割に応じて、異なる組み合わせが四次(ホモ二量体/ヘテロ二量体)構造形成に多様な影響を及ぼすであろうことを述べなければならない。アミノ酸ヒスチジン(His)は、中性pHでは正電荷であり、そしてしたがってHisに対する突然変異もまた意図される。しかし、負電荷残基(AspまたはGlu)をHisに突然変異させると、側鎖体積が増加し、これが立体問題を引き起こす可能性もある。さらに、ヒスチジン・
プロトンドナーおよびアクセプター型は、局所環境に応じる。設計戦略中、これらの問題を考慮に入れなければならない。
1997)。「ノブを穴に」突然変異体に関しては、示差走査熱量測定実験において、エンタルピーの減少もまた観察された。
。好ましくは、CH3ドメインに関して上述するものと類似の静電的ステアリング技術を用いて、これを達成する。
接合部分内のカッパ軽鎖−重鎖接触を表5に示す。
本実施例は、静電的ステアリング効果を用いて、ホモ二量体化を不利にしつつ、ヘテロ二量体化を有利にするように、CH3ドメインを操作可能であることを立証する。CH3ドメイン接合部分に電荷残基突然変異を有する、図8(a)に示すようなマキシボディ−ダミーFc構築物を作製した。SDSポリアクリルアミドゲル電気泳動を通じて、ホモ二
量体およびヘテロ二量体収量の形成を評価した。マキシボディは、ダミーFcに比較して、より高い分子量を有するため、ヘテロ二量体(マキシボディ−ダミーFc)およびホモ二量体(マキシボディ−マキシボディおよびダミーFc−ダミーFc)は、SDS−PAGE上で異なる移動度を有し、これによって、多様な対形成の同定が容易になる(図8(b))。
と一致するKabat番号付け系(Kabatら, Sequences of Proteins of Immunological Interest, National Institutes of Health, Bethesda, Md., 第5版, [1991])を用いた位、そして次いで一文字暗号で示す置換残基によって、突然変異を示す。これらの2つの構築物中で用いるFc配列は、ヒトIgG1非(a)アロタイプに由来し、これは356位でGluおよび358位でMetを有する。結晶構造由来のCH3配列は異なるIgG1アロタイプ由来であり、これは356位でAspおよび368位でLeuを有する。
K409近くに位置する電荷残基、例えばK360およびK392で、さらなる突然変異を導入した際、ヘテロ二量体形成のさらなる増加が観察された(図10)。例えば、ダミーFc上のK409D;K392DとM315マキシボディ上のD399’Kを組み合
わせると、ホモ二量体に対するヘテロ二量体の比の増加が示され、これはおそらくFcホモ二量体の破壊のためである。Fc単量体のサイズに対応する25KDのバンドが、K409D;K392DダミーFcを用いたすべてのトランスフェクション上で検出された(データ未提示)。M315マキシボディのD399’K変異体に加えてD356’KまたはD357’Kなどの別の突然変異を付加すると、さらなる改善が示された。ダミーFc上のK409D;K392DとM315マキシボディ上のD399’K;D356’Kを組み合わせると、ヘテロ二量体がほぼ排他的に形成された。K409D;K392D/D399’K;D357’KおよびK409D;K370D/D399’K;D357’Kなどの他の組み合わせもまた、K409D/D399’K変異体より有意な改善を提供した。
実施例2
本実施例は、特定の三重電荷対突然変異が、単独で発現された場合にホモ二量体を形成不能であるが、同時発現された場合にヘテロ二量体を形成可能であったことを立証する。実施例1に記載するように、突然変異体を作製し、そして細胞をトランスフェクションした。構築物を同時トランスフェクションする際には、1:1のプラスミド比を用いた。結果を図11に示す。ヤギ抗ヒトFc HRPコンジュゲート化抗体を用いたウェスタンブロットによって、ヘテロ二量体およびホモ二量体を検出した。興味深いことに、正電荷残基を負電荷残基に変化させた(K409D、K392D、K370DまたはK409D、K392D、K439D)三重突然変異を有するFc含有分子は、単独で発現させた際、検出不能であった。同様に、負電荷残基を正電荷残基に変化させた(D399K、E356K、E357K)三重突然変異を有するFc含有分子は、単独で発現させた際、検出不
能であった。しかし、反対の電荷極性の突然変異を有するFc含有分子と同時発現させると、ヘテロ二量体のみが検出された。
ある態様において、本発明は以下であってもよい。
[態様1]集合して、ヘテロ二量体形成を促進するように操作された接合部分(interface)を形成する、第一のCH3含有ポリペプチドおよび第二のCH3含有ポリペプチドを含むヘテロ二量体タンパク質を調製する方法であって、前記の第一のCH3含有ポリペプチドおよび前記の第二のCH3含有ポリペプチドが、接合部分内に、ホモ二量体形成にとって静電的に不利であるが、ヘテロ二量体形成にとって静電的に有利である、1以上の荷電アミノ酸を含み:
(a)第一のCH3含有ポリペプチドをコードする核酸および第二のCH3含有ポリペプチドを含む核酸を含む宿主細胞を培養し、ここで培養された宿主細胞が第一および第二のCH3含有ポリペプチドを発現し;そして
(b)宿主細胞培養からヘテロ二量体タンパク質を回収する
工程を含む、前記方法。
[態様2]ヘテロ二量体タンパク質がFc領域を含む、態様1の方法。
[態様3]Fc領域がIgG Fc領域を含む、態様2の方法。
[態様4]IgG Fc領域がヒトIgG Fc領域を含む、態様3の方法。
[態様5]ヒトIgG領域がIgG1 Fc領域を含む、態様4の方法。
[態様6]IgG領域がIgG2 Fc領域を含む、態様4の方法。
[態様7]IgG領域がIgG3 Fc領域を含む、態様4の方法。
[態様8]IgG領域がIgG4 Fc領域を含む、態様4の方法。
[態様9]Fc領域が、IgA、IgE、IgD、またはIgM Fc領域を含む、態様2の方法。
[態様10]野生型ヒトIgG配列中の1以上の正電荷アミノ酸が1以上の負電荷アミノ酸で置き換えられるように、第一のCH3含有ポリペプチドまたは第二のCH3含有ポリペプチドが、野生型ヒトIgGと異なるポリペプチド配列を含む、態様4の方法。
[態様11]正電荷アミノ酸が、リジン、ヒスチジン、およびアルギニンからなる群より選択される、態様10の方法。
[態様12]負電荷アミノ酸が、アスパラギン酸およびグルタミン酸からなる群より選択される、態様10の方法。
[態様13]野生型ヒトIgG配列中の1以上の負電荷アミノ酸が1以上の正電荷アミノ酸で置き換えられるように、第一のCH3含有ポリペプチドまたは第二のCH3含有ポリペプチドが、野生型ヒトIgGと異なるポリペプチド配列を含む、態様10の方法。
[態様14]正電荷アミノ酸が、リジン、ヒスチジン、およびアルギニンからなる群より選択される、態様13の方法。
[態様15]負電荷アミノ酸が、アスパラギン酸およびグルタミン酸からなる群より選択される、態様13の方法。
[態様16]野生型ヒトIgG1配列中の1以上の正電荷アミノ酸が1以上の負電荷アミノ酸で置き換えられるように、IgG1 Fcが、野生型ヒトIgG1と異なるポリペプチド配列を有する第一のCH3含有ポリペプチドまたは第二のCH3含有ポリペプチドを含む、態様5の方法。
[態様17]第一のCH3含有ポリペプチドが負電荷アミノ酸でのリジンの置換を含む、態様16の方法。
[態様18]リジンが、Lys409、Lys392、Lys439、およびLys370からなる群より選択される、態様17の方法。
[態様19]野生型ヒトIgG1配列中の1以上の負電荷アミノ酸が1以上の正電荷アミノ酸で置き換えられるように、IgG1 Fcが、野生型ヒトIgG1と異なるポリペプチド配列を有する第一のCH3含有ポリペプチドまたは第二のCH3含有ポリペプチドを含む、態様5の方法。
[態様20]第一のCH3含有ポリペプチドが正電荷アミノ酸でのアスパラギン酸の置換を含む、態様19の方法。
[態様21]アスパラギン酸が、Asp399およびAsp356からなる群より選択される、態様20の方法。
[態様22]第一のCH3含有ポリペプチドが正電荷アミノ酸でのグルタミン酸の置換を含む、態様19の方法。
[態様23]グルタミン酸がGlu357である、態様22の方法。
[態様24]第一のCH3含有ポリペプチドが負電荷アミノ酸でのLys409の置換を含み、そして第二のCH3含有ポリペプチドが、正電荷アミノ酸でのAsp399、Asp356、またはGlu357の置換を含む、態様18の方法。
[態様25]第一のCH3含有ポリペプチドが負電荷アミノ酸でのLys392の置換を含み、そして第二のCH3含有ポリペプチドが、正電荷アミノ酸でのAsp399、Asp356、またはGlu357の置換を含む、態様18の方法。
[態様26]第一のCH3含有ポリペプチドが負電荷アミノ酸でのLys439の置換を含み、そして第二のCH3含有ポリペプチドが、正電荷アミノ酸でのAsp399、Asp356、またはGlu357の置換を含む、態様18の方法。
[態様27]第一のCH3含有ポリペプチドが負電荷アミノ酸でのLys370の置換を含み、そして第二のCH3含有ポリペプチドが、正電荷アミノ酸でのAsp399、Asp356、またはGlu357の置換を含む、態様18の方法。
[態様28]第一のCH3含有ポリペプチドが正電荷アミノ酸でのAsp399の置換を含み、そして第二のCH3含有ポリペプチドが、負電荷アミノ酸でのLys409、Lys439、Lys370、またはLys392の置換を含む、態様20の方法。
[態様29]第一のCH3含有ポリペプチドが正電荷アミノ酸でのAsp356の置換を含み、そして第二のCH3含有ポリペプチドが、負電荷アミノ酸でのLys409、Lys439、Lys370、またはLys392の置換を含む、態様20の方法。
[態様30]第一のCH3含有ポリペプチドが正電荷アミノ酸でのGlu357の置換を含み、そして第二のCH3含有ポリペプチドが、負電荷アミノ酸でのLys409、Lys439、Lys370、またはLys392の置換を含む、態様23の方法。
[態様31]第一のCH3含有ポリペプチドが抗体重鎖である、態様1の方法。
[態様32]第二のCH3含有ポリペプチドが抗体重鎖である、態様1の方法。
[態様33]宿主細胞が1以上の抗体軽鎖を発現する、態様1の方法。
[態様34]ヘテロ二量体タンパク質が、抗体、二重特異性抗体、単一特異性一価抗体、二重特異性マキシボディ、モノボディ、ペプチボディ、二重特異性ペプチボディ、一価ペプチボディ、および受容体融合タンパク質からなる群より選択される、態様1の方法。
[態様35]第一のCH3含有ポリペプチドをコードする核酸および第二のCH3含有ポリペプチドを含む核酸を含む宿主細胞であって、第一のCH3含有ポリペプチドおよび第二のCH3含有ポリペプチドが集合して、ヘテロ二量体形成を促進するように操作された接合部分を形成し、そして前記の第一のCH3含有ポリペプチドおよび前記の第二のCH3含有ポリペプチドが、接合部分内に、ホモ二量体形成にとって静電的に不利であるが、ヘテロ二量体形成にとって静電的に有利である、1以上の荷電アミノ酸を含む、前記宿主細胞。
[態様36]第一のCH3含有ポリペプチドをコードする核酸および第二のCH3含有ポリペプチドを含む核酸を含む組成物であって、第一のCH3含有ポリペプチドおよび第二のCH3含有ポリペプチドが集合して、ヘテロ二量体形成を促進するように操作された接合部分を形成し、そして前記の第一のCH3含有ポリペプチドおよび前記の第二のCH3含有ポリペプチドが、接合部分内に、ホモ二量体形成にとって静電的に不利であるが、ヘテロ二量体形成にとって静電的に有利である、1以上の荷電アミノ酸を含む、前記組成物。
[態様37]集合して、ヘテロ二量体形成を促進するように操作された接合部分を形成する、第一のCH3含有ポリペプチドおよび第二のCH3含有ポリペプチドを含むヘテロ二量体タンパク質であって、前記の第一のCH3含有ポリペプチドおよび前記の第二のCH3含有ポリペプチドが、接合部分内に、ホモ二量体形成にとって静電的に不利であるが、ヘテロ二量体形成にとって静電的に有利である、1以上の荷電アミノ酸を含む、前記ヘテロ二量体タンパク質。
[態様38]Fc領域を含む、態様37のヘテロ二量体タンパク質。
[態様39]Fc領域がIgG Fc領域を含む、態様38のヘテロ二量体タンパク質。
[態様40]IgG Fc領域がヒトIgG Fc領域を含む、態様39のヘテロ二量体タンパク質。
[態様41]ヒトIgG領域がIgG1 Fc領域を含む、態様40のヘテロ二量体タンパク質。
[態様42]IgG領域がIgG2 Fc領域を含む、態様40のヘテロ二量体タンパク質。
[態様43]IgG領域がIgG3 Fc領域を含む、態様40のヘテロ二量体タンパク質。
[態様44]IgG領域がIgG4 Fc領域を含む、態様40のヘテロ二量体タンパク質。
[態様45]Fc領域が、IgA、IgE、IgD、またはIgM Fc領域を含む、態様38のヘテロ二量体タンパク質。
[態様46]野生型ヒトIgG配列中の1以上の正電荷アミノ酸が1以上の負電荷アミノ酸で置き換えられるように、第一のCH3含有ポリペプチドまたは第二のCH3含有ポリペプチドが、野生型ヒトIgGと異なるポリペプチド配列を含む、態様40のヘテロ二量体タンパク質。
[態様47]正電荷アミノ酸が、リジン、ヒスチジン、およびアルギニンからなる群より選択される、態様46のヘテロ二量体タンパク質。
[態様48]負電荷アミノ酸が、アスパラギン酸およびグルタミン酸からなる群より選択される、態様46のヘテロ二量体タンパク質。
[態様49]野生型ヒトIgG配列中の1以上の負電荷アミノ酸が1以上の正電荷アミノ酸で置き換えられるように、第一のCH3含有ポリペプチドまたは第二のCH3含有ポリペプチドが、野生型ヒトIgGと異なるポリペプチド配列を含む、態様46のヘテロ二量体タンパク質。
[態様50]正電荷アミノ酸が、リジン、ヒスチジン、およびアルギニンからなる群より選択される、態様49のヘテロ二量体タンパク質。
[態様51]負電荷アミノ酸が、アスパラギン酸およびグルタミン酸からなる群より選択される、態様49のヘテロ二量体タンパク質。
[態様52]野生型ヒトIgG1配列中の1以上の正電荷アミノ酸が1以上の負電荷アミノ酸で置き換えられるように、IgG1 Fcが、野生型ヒトIgG1と異なるポリペプチド配列を有する第一のCH3含有ポリペプチドまたは第二のCH3含有ポリペプチドを含む、態様41のヘテロ二量体タンパク質。
[態様53]第一のCH3含有ポリペプチドが負電荷アミノ酸でのリジンの置換を含む、態様52のヘテロ二量体タンパク質。
[態様54]リジンが、Lys409、Lys392、Lys439、およびLys370からなる群より選択される、態様53のヘテロ二量体タンパク質。
[態様55]野生型ヒトIgG1配列中の1以上の負電荷アミノ酸が1以上の正電荷アミノ酸で置き換えられるように、IgG1 Fcが、野生型ヒトIgG1と異なるポリペプチド配列を有する第一のCH3含有ポリペプチドまたは第二のCH3含有ポリペプチドを含む、態様41のヘテロ二量体タンパク質。
[態様56]第一のCH3含有ポリペプチドが正電荷アミノ酸でのアスパラギン酸の置換を含む、態様55のヘテロ二量体タンパク質。
[態様57]アスパラギン酸が、Asp399およびAsp356からなる群より選択される、態様56のヘテロ二量体タンパク質。
[態様58]第一のCH3含有ポリペプチドが正電荷アミノ酸でのグルタミン酸の置換を含む、態様55のヘテロ二量体タンパク質。
[態様59]グルタミン酸がGlu357である、態様58のヘテロ二量体タンパク質。
[態様60]第一のCH3含有ポリペプチドが負電荷アミノ酸でのLys409の置換を含み、そして第二のCH3含有ポリペプチドが、正電荷アミノ酸でのAsp399、Asp356、またはGlu357の置換を含む、態様54のヘテロ二量体タンパク質。
[態様61]第一のCH3含有ポリペプチドが負電荷アミノ酸でのLys392の置換を含み、そして第二のCH3含有ポリペプチドが、正電荷アミノ酸でのAsp399、Asp356、またはGlu357の置換を含む、態様54のヘテロ二量体タンパク質。
[態様62]第一のCH3含有ポリペプチドが負電荷アミノ酸でのLys439の置換を含み、そして第二のCH3含有ポリペプチドが、正電荷アミノ酸でのAsp399、Asp356、またはGlu357の置換を含む、態様54のヘテロ二量体タンパク質。
[態様63]第一のCH3含有ポリペプチドが負電荷アミノ酸でのLys370の置換を含み、そして第二のCH3含有ポリペプチドが、正電荷アミノ酸でのAsp399、Asp356、またはGlu357の置換を含む、態様54のヘテロ二量体タンパク質。
[態様64]第一のCH3含有ポリペプチドが正電荷アミノ酸でのAsp399の置換を含み、そして第二のCH3含有ポリペプチドが、負電荷アミノ酸でのLys409、Lys439、Lys370、またはLys392の置換を含む、態様57のヘテロ二量体タンパク質。
[態様65]第一のCH3含有ポリペプチドが正電荷アミノ酸でのAsp356の置換を含み、そして第二のCH3含有ポリペプチドが、負電荷アミノ酸でのLys409、Lys439、Lys370、またはLys392の置換を含む、態様57のヘテロ二量体タンパク質。
[態様66]第一のCH3含有ポリペプチドが正電荷アミノ酸でのGlu357の置換を含み、そして第二のCH3含有ポリペプチドが、負電荷アミノ酸でのLys409、Lys439、Lys370、またはLys392の置換を含む、態様59のヘテロ二量体タンパク質。
[態様67]第一のCH3含有ポリペプチドが抗体重鎖である、態様37のヘテロ二量体タンパク質。
[態様68]第二のCH3含有ポリペプチドが抗体重鎖である、態様37のヘテロ二量体タンパク質。
[態様69]ヘテロ二量体タンパク質が1以上の抗体軽鎖をさらに含む、態様37のヘテロ二量体タンパク質。
[態様70]抗体、二重特異性抗体、単一特異性一価抗体、二重特異性マキシボディ、モノボディ、ペプチボディ、二重特異性ペプチボディ、一価ペプチボディ、および受容体融合タンパク質からなる群より選択される、態様37のヘテロ二量体タンパク質。
[態様71]抗体のCH3領域を含むポリペプチドであって、野生型CH3中の1以上の正電荷アミノ酸が1以上の負電荷アミノ酸で置き換えられるように、CH3領域が、野生型CH3領域と異なるポリペプチド配列を含み、野生型CH3領域を含むポリペプチドに比較して、ホモ二量体を形成する能力が減少している、前記ポリペプチド。
[態様72]抗体のCH3領域を含むポリペプチドであって、野生型CH3中の1以上の負電荷アミノ酸が1以上の正電荷アミノ酸で置き換えられるように、CH3領域が、野生型CH3領域と異なるポリペプチド配列を含み、野生型CH3領域を含むポリペプチドに比較して、ホモ二量体を形成する能力が減少している、前記ポリペプチド。
[態様73]CH2領域をさらに含む、態様71のポリペプチド。
[態様74]CH2領域をさらに含む、態様72のポリペプチド。
[態様75]抗体重鎖を含む、態様73のポリペプチド。
[態様76]抗体重鎖を含む、態様74のポリペプチド。
[態様77]態様75のポリペプチドを含む抗体。
[態様78]態様76のポリペプチドを含む抗体。
[態様79]態様71〜76のいずれかのポリペプチドをコードする単離核酸。
[態様80]プロモーターに機能可能であるように連結された態様79の単離核酸を含む、発現ベクター。
[態様81]態様80の発現ベクターを含有する宿主細胞。
[態様82]態様71〜76のいずれかのポリペプチドを含む、薬学的組成物。
Claims (13)
- 集合して、ヘテロ二量体形成を促進するように操作された接合部分(interface)を形成する、第一のCH3含有ポリペプチドおよび第二のCH3含有ポリペプチドを含むヘテロ二量体タンパク質を調製する方法であって、
前記の第一のCH3含有ポリペプチドおよび前記の第二のCH3含有ポリペプチドが、接合部分内に、ホモ二量体形成にとって静電的に不利であるが、ヘテロ二量体形成にとって静電的に有利である、1以上の荷電アミノ酸を含み:
(a)第一のCH3含有ポリペプチドをコードする核酸および第二のCH3含有ポリペプチドを含む核酸を含む宿主細胞を培養し、ここで培養された宿主細胞が第一および第二のCH3含有ポリペプチドを発現し;そして
(b)宿主細胞培養からヘテロ二量体タンパク質を回収する
工程を含み、
前記の第一のCH3含有ポリペプチドおよび前記の第二のCH3含有ポリペプチドのそれぞれはIgGのCH3含有ポリペプチドであり、
第一のCH3含有ポリペプチドが、392位のアミノ酸残基の負電荷アミノ酸での置換を含み、第二のCH3含有ポリペプチドが、399位のアミノ酸残基の正電荷アミノ酸での置換を含む、
前記方法。 - 第一のCH3含有ポリペプチドが、370位及び/又は409位のアミノ酸残基の負電荷アミノ酸での置換を含む、請求項1に記載の方法。
- 第二のCH3含有ポリペプチドが、356位、及び357位からなる群より選択される位置のアミノ酸残基の正電荷アミノ酸での置換を含む、請求項1又は2に記載の方法。
- 第一のCH3含有ポリペプチドにおける置換前の392位のアミノ酸残基がリジン又はアスパラギンである、請求項1〜3のいずれか1項に記載の方法。
- 第一のCH3含有ポリペプチドにおける置換前の370位のアミノ酸残基がリジンである、請求項2〜4のいずれか1項に記載の方法。
- 第一のCH3含有ポリペプチドにおける置換前の409位のアミノ酸残基がリジンである、請求項2〜5のいずれか1項に記載の方法。
- 第二のCH3含有ポリペプチドにおける置換前の356位のアミノ酸残基がグルタミン酸又はアスパラギン酸である、請求項3〜6のいずれか1項に記載の方法。
- 第二のCH3含有ポリペプチドにおける置換前の357位のアミノ酸残基がグルタミン酸である、請求項3〜7のいずれか1項に記載の方法。
- 第二のCH3含有ポリペプチドにおける置換前の399位のアミノ酸残基がアスパラギン酸である、請求項3〜8のいずれか1項に記載の方法。
- 負電荷アミノ酸がアスパラギン酸である、請求項1〜9のいずれか1項に記載の方法。
- 正電荷アミノ酸がリジンである、請求項3〜10のいずれか1項に記載の方法。
- ヘテロ二量体タンパク質がヒトIgG Fc領域を含む、請求項1〜11のいずれか1項に記載の方法。
- ヒトIgG Fc領域がIgG1 Fc領域を含む、請求項12に記載の方法。
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AU2009204501A1 (en) | 2009-07-16 |
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