JP4831436B2 - クロマトグラフィーリガンド - Google Patents
クロマトグラフィーリガンド Download PDFInfo
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- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
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- C07K16/065—Purification, fragmentation
Description
用語「抗体」及び「免疫グロブリン」は、本明細書中で互換的に使用される。
式中、
R1は、置換又は非置換芳香族環系、例えばフェニル基であり、
R2は炭素原子数0〜4の炭化水素鎖であり、
R3は炭素原子数1〜3の炭化水素鎖であり、
R4は炭素原子数1〜5の炭化水素鎖であり、
R5はOH又はHである。
図1は、ビーズ形態の担体に窒素原子を経由して固定されたプロトタイプリガンドであるN−ベンジル−N−メチルエタノールアミンを示す。左側には図式的に描いたリンカーと、右側には実例としての親水性リンカーとカップリングしたリガンドを示す。実験の部で、プロトタイプリガンドを6%アガロースマトリックスであるSepharose(商標)6FF(スウェーデン、Uppsala、GE Healthcare)にカップリングした。
本発明による分離マトリックスの調製
BMEA Sepharose Fast Flowの調製
架橋アガロースゲル(Sepharose(商標)6 Fast Flow、スウェーデン、Uppsala、GE Healthcare)から出発する、本発明による分離マトリックスの調製方法の一実施形態を以下に示す。
Sepharose 6 Fast Flowをアリルグリシジルエーテルで次のように活性化した。即ち、100mlのSepharose 6 Fast Flowを吸引乾燥し、0.3gのNaBH4、12gのNa2SO4及び35mlの50%NaOH水溶液と混合した。混合物を50℃で1時間撹拌した。100mlのアリルグリシジルエーテルを添加した後、懸濁液を激しく撹拌しながら50℃で更に16時間保持した。混合物を濾過した後、ゲルを500mlの蒸留水、500mlのエタノール、200mlの蒸留水、200mlの0.2M酢酸及び500mlの蒸留水で順次洗浄した。
50mlのアリル活性化Sepharose 6 Fast Flow(アリル基0.22ミリモル/ml排水ゲル)、1gの酢酸ナトリウム及び15mlの蒸留水からなる撹拌懸濁液に、臭素を黄色が持続するまで添加した。次いで、ギ酸ナトリウムを懸濁液が完全に脱色されるまで添加した。反応混合物を濾過し、ゲルを500mlの蒸留水で洗浄した。次いで、活性化ゲルを反応容器に直ちに移送し、N−ベンジル−N−メチルエタノールアミンと更に反応させた。
アミン基の窒素原子を経由してマトリックスにアミン基を直接導入した。典型的な手順において、マトリックスへのカップリングは、アリル基の臭素化及び塩基性条件下での求核置換により実現された。25mlの臭素活性化ゲル(アリル基0.22ミリモル/ml排水ゲル)を、N−ベンジル−N−メチルエタノールアミン(16.0ml)の溶液を含む反応ガラス瓶に移した。5mlの水を添加し、反応溶液のpHを水酸化ナトリウム溶液で12.0に調整した。反応物を撹拌下に50℃で16時間保持した。反応混合物を濾過した後、ゲルを、10mlの蒸留水で3回、10mlの0.5HCl水で3回、最後に10mlの蒸留水で3回、順次洗浄した。BMEA Sepharose Fast Flowゲルが、アミン0.15ミリモル/mlゲルの置換度で得られた。
通過液中の抗体の精製
実施例2A:実験配置
非結合条件下で、約50mgのmAb1を含む試料を、プロトタイプ901035A(N−ベンジル−N−メチルエタノールアミン)上に約5及び12mS/cmで注入した。5、10及び15カラム体積(CV)時に通過液画分(FT)を集めた。溶出ピークからの画分をプールした。FT画分を、HCP及びプロテインAの含有量について分析した。
カラム及びゲルは、スウェーデン、Uppsala、GE Healthcareから入手した。
使用する化学薬品はすべて分析級とした。水はMilliQで濾過した。
Q Sepharose(商標)Fast Flow(FF)(スウェーデン、Uppsala、GE Healthcare)。分離マトリックスのリガンドは、下表1に記載した通りのプロトタイプである。
MAb1及びMAb2と表示され、それぞれ1.46及び1.50の吸光係数を有する2つの異なるヒト化IgG抗体、サブクラス1を使用した。双方の抗体とも、CHO培養で発現させ、続いて本発明の実験に先立って従来からのプロテインAアフィニティークロマトグラフィーを使用して精製した。
式中、
A280は280nmでの吸光度であり、
ε(mL・mg−1・cm−1)は特定のタンパク質に対する吸光係数であり、
C(mg/mL)はタンパク質の濃度であり、
l(cm)は光路長である。
緩衝液は、25mM Bis−Tris、pH6.0又は6.5とした。所望される導電率、約5又は12mS/cmに応じて、35又は100mMのNaClを含めた。溶出緩衝液(B−緩衝液)は、25mM Bis−Tris、0.5M NaCl、pH6.5とした。流速は0.5mL/分(150cm/時間)とした。
A−緩衝液は25mM Bis−Tris、pH6.0とした。導電率は、50mM NaClを添加して約7mS/cmとし、B−緩衝液は、0.5M酢酸ナトリウム、pH4.0とした。流速は0.5mL/分(150cm/時間)とした。試料濃度は、MAbを4mg/mL、rPrAを0.04mg/mL(1%(w/w)に相当)とした。
選択した画分を、800μLのSPA試料希釈液+200μL試料の比率でSPA試料希釈液と混合した。混合後、画分を加熱ブロック上、99℃で10分間加熱し、次いで、再混合した。次いで、試料を組換えプロテインAについて分析した。
試料(最小で600μL)をHCP含有量について分析した。検出下限は10ng/mLである。
プロトタイプリガンドN−ベンジル−N−メチルエタノールアミン(901035A)で精製したMAb−1含有試料
50mgのMAb1を含む試料を、Sepharose(商標)6FFに固定化し、上記の実施例1に記載した通りに調製したN−ベンジル−N−メチルエタノールアミン(901035A)、Sepharose(商標)6FFに固定化したN,N−ジメチルベンジルアミン(901035B)及び対照マトリックスQ Sepharose(商標)FFに、25mM Bis−Tris、100mM NaCl(〜12mS/cm)、pH6.5で適用した。溶出は、25mM Bis−Tris、0.5M NaCl、pH6.5で実施した。
プロトタイプリガンド、N−ベンジル−N−メチルエタノールアミンでの、MAb1及び組換えプロテインA(rPrA)を含む試料からの通過液中のMAb1の精製
この実施例では、Ab1−rプロテインAを含む試料についてのプロトタイプでのクロマトグラフィーを実施した。A−緩衝液は、25mM Bis−Tris、50mM NaCl、pH6.0とした。導電率は約7mS/cmであった。B−緩衝液は、0.5M酢酸ナトリウム、pH4.0とした。流速は0.5mL/分(150cm/時間)であった。試料は、mAb1が4mg/mL、rプロテインAが1%(w/w)の濃度の、10mgのmAb1、0.10mgのrPrAとした。結果を図3に示す。
吸着方式
4A)実験配置
吸着方式でのBMEA Sepharose Fast Flow(BMEA;N−ベンジル−N−メチルエタノールアミン)の選択性を試験するために、ヒトIgG及び8種の異なるタンパク質の保持時間を試験した。結果を、市販の陰イオン交換体Q Sepharose Fast Flowと比較した。試験方法の原理は、タンパク質を、A−緩衝液(緩衝液成分としてピペラジンを含む)で平衡化したHR5/5カラム(Sepharose(商標)Fast Flowに固定したBMEAリガンドを含む)中に注入するものである。タンパク質の溶出には塩勾配を使用した(下記の方法を参照のこと)。
カラム及びQ Sepharose Fast Flowは、スウェーデン、Uppsala、GE Healthcareから入手した。
HR 5/5(商標):カタログ番号18−0338−01 カラム体積CV=1mL。
クロマトグラフィー装置 AKTAExplorer(商標)10。
タンパク質、卵白アルブミン、β−ラクトグロブリン、ウシ血清アルブミン、α−ラクトアルブミン、ミオグロビン、ラクトフェリン、リボヌクレアーゼA及びシトクロムCはSigmaから購入し、ヒトIgG(Gammanorm)はOctapharmaから購入した。タンパク質は、A−緩衝液に1〜10mg/mlの濃度で溶解した。Q Sepharose Fast Flowはスウェーデン、Uppsala、GE Healthcareから入手した。使用したすべての化学薬品は分析級であり、水はMilliQで濾過した。
100μlの試料用液を適用する前に、0.6ml/分の流速のA−緩衝液でカラムを平衡化した。1回に1種のタンパク質のみを分析した。緩衝液Aから緩衝液Bまで21カラム容積の勾配容積を用いる線形勾配によってタンパク質を溶出した(下記の方法を参照のこと)。緩衝液Aは、25mMピペラジン、pH10.0とし、緩衝液Bは、25mMピペラジン、1.0M NaCl、pH10.0とした。ラン中はすべて280nmでの吸光度を検出した。
BMEAリガンドが、免疫グロブリンと選択的に相互作用するか否かを立証するために、新規媒体を充填した1mlカラム(HR5/5)にヒトIgGを適用した。更に、タンパク質卵白アルブミン、β−ラクトグロブリン、ウシ血清アルブミン、α−ラクトアルブミン、ミオグロビン、ラクトフェリン、リボヌクレアーゼA及びシトクロムCも適用した。結果を、Q Sepharose Fast Flowで観察されたタンパク質の保持時間と比較した。Q Sepharose Fast Flowは、強陰イオン交換体であり、それは同一の担体マトリックス(担体材料、ビーズ径、細孔径、細孔容積、充填方法など)を有し、本質的に同一の置換度(イオン交換容量として測定して)を有するので、対照の陰イオン交換体として使用される。表1から明らかなように、BMEA Sepharose Fast Flowは、調べたすべてのタンパク質を、Q Sepharose Fast Flowに比べてより強力に遅延させた。更に、IgGは、BMEA Sepharose Fast Flowで最も長い保持時間を与えるタンパク質であった(表1)。これは、Q Sepharose Fast Flowに対するよりもBMEA媒体に対するはるかにより強い結合を反映している。BMEA Sepharose Fast Flowを使用すると、Q Sepharose Fast Flowに比べ、IgGの保持時間が27.3分増加する(表1)。これらの結果は、BMEA Sepharose Fast Flowを使用して、選択的方式でIgGを捕捉し、溶出できることを明瞭に示している。
Claims (10)
- 次式で定義されるクロマトグラフィーリガンドをそのアミン基を介して担体にカップリングしてなる分離マトリックス。
R1−R2−N(R3)−R4−R5
式中、
R1は、置換又は非置換フェニル基であり、
R2は炭素原子数0〜4の炭化水素鎖であり、
R3は炭素原子数1〜3の炭化水素鎖であり、
R4は炭素原子数1〜5の炭化水素鎖であり、
R5はOH又はHである。 - R1、R2、R3及びR4の1以上がOHで置換されている、請求項1記載の分離マトリックス。
- R1が非置換フェニル基である、請求項1又は請求項2記載の分離マトリックス。
- R2が−CH2−である、請求項1乃至請求項3のいずれか1項記載の分離マトリックス。
- R3が−CH3である、請求項1乃至請求項4のいずれか1項記載の分離マトリックス。
- R4が−CH2−CH2−CH2−又は−CH2−CH2−である、請求項1乃至請求項5のいずれか1項記載の分離マトリックス。
- 前記リガンドがN−ベンジル−N−メチルエタノールアミンを含む、請求項1乃至請求項6のいずれか1項記載の分離マトリックス。
- 前記担体が粒子を含む、請求項1乃至請求項7のいずれか1項記載の分離マトリックス。
- 前記担体が球状粒子を含む、請求項1乃至請求項7のいずれか1項記載の分離マトリックス。
- 前記担体がメンブラン構造を含む、請求項1乃至請求項7のいずれか1項記載の分離マトリックス。
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