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首页> 外文期刊>Biotechnology Progress >Enantioselective affinity chromatography of a chiral drug by crystalline and carrier-bound antibody fab fragment
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Enantioselective affinity chromatography of a chiral drug by crystalline and carrier-bound antibody fab fragment

机译：通过结晶和载体结合的抗体fab片段对手性药物进行对映选择性亲和层析

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摘要

An antibody Fab fragment, ENA5His, capable of enantioselective affinity chromatographic separation of a chiral drug, finrozole, was stabilized against organic solvents by chemical cross-linking. High concentration of methanol is needed to release the bound drug from the antibody fragment. However, in native form the antibody fragment is unstable at these conditions. We used cross-linked protein crystal technology to stabilize the antibody fragment molecule. Glutaraldehyde cross-linked ENA5His crystals (CLAC) packed in a column separated pure enantiomers from the racemic mixture of the drug. CLAC was totally stable at the elution conditions, enabling reuse of the immunoaffinity column packed with CLAC. However, the specific drug enantiomer binding capacity of CLAC was only 50% of the corresponding capacity of immobilized ENA5His. We were also able to cross-link immobilized ENA5His by glutaraldehyde. This method produced a protein matrix with high activity and stability in the elution conditions.
机译：能够通过手性药物芬洛唑进行对映选择性亲和色谱分离的抗体Fab片段ENA5His通过化学交联稳定了有机溶剂。需要高浓度的甲醇以从抗体片段释放结合的药物。但是，天然形式的抗体片段在这些条件下不稳定。我们使用了交联的蛋白质晶体技术来稳定抗体片段分子。戊二醛交联的ENA5His晶体（CLAC）装在色谱柱中，从药物的外消旋混合物中分离出纯对映体。 CLAC在洗脱条件下是完全稳定的，可以重新使用装有CLAC的免疫亲和柱。但是，CLAC的特异性药物对映体结合能力仅为固定化ENA5His相应能力的50％。我们还能够通过戊二醛交联固定化的ENA5His。该方法产生了在洗脱条件下具有高活性和稳定性的蛋白质基质。

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