3P049 Multimodal chromatography of proteins in arginine solutions(01C. Protein: Property,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))

A. Hirano, T. Arakawa, T. Kameda
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引用次数: 0

Abstract

Arginine is effective in elution of proteins from chromatography columns. In this study, effects of arginine on the elution from multimodal chromatography columns, the resins of which have multiple functional groups, were examined using bovine serum albumin and a monoclonal antibody against interleukin-8. The resins used here were Capto MMC and Capto adhere, which are multimodal cation and anion exchangers, respectively. As expected, arginine effectively eluted the proteins from the columns. Mechanism of the elution was examined by molecular dynamics simulations. The results showed that the affinity of arginine was primarily associated with electrostatic interaction for Capto MMC and with hydrophobic and π-π interactions as well as hydrogen bonding for Capto adhere.
精氨酸溶液中蛋白质的多模态色谱法(01C)。蛋白质:性质,海报,第52届日本生物物理学会年会(BSJ2014)
精氨酸对色谱柱中蛋白质的洗脱是有效的。本研究利用牛血清白蛋白和抗白细胞介素-8单克隆抗体,研究了精氨酸对多模态色谱柱洗脱的影响。本文使用的树脂分别为Capto MMC和Capto粘接树脂,它们分别是多模态阳离子交换剂和阴离子交换剂。不出所料,精氨酸有效地洗脱了柱上的蛋白质。通过分子动力学模拟研究了其洗脱机理。结果表明,精氨酸的亲和力主要与Capto MMC的静电相互作用有关,与Capto粘附体的疏水、π-π相互作用和氢键相互作用有关。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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