Literature DB >> 24642397

Interaction of arginine with Capto MMC in multimodal chromatography.

Atsushi Hirano1, Tsutomu Arakawa2, Tomoshi Kameda3.   

Abstract

This study highlights the ability of arginine to elute bovine serum albumin (BSA) and a monoclonal antibody against interleukin-8 (mAb-IL8) from Capto MMC, which is a multimodal cation exchanger. Arginine provides high recovery of monomeric BSA from Capto MMC chromatography columns at yields similar to NaCl elution, and oligomeric BSA was more readily eluted by arginine than by NaCl. The effectiveness of arginine as an eluent also enabled the separation of monomeric BSA from the oligomeric forms. The purification of mAb-IL8 was successfully achieved using Capto MMC chromatography and arginine as the eluent. The mechanism of the effects of arginine on protein elution was determined by calculating the binding free energy between arginine and Capto MMC using molecular dynamics simulations. The overall affinity of arginine for Capto MMC was associated with electrostatic interactions. However, additional affinities contributed by hydrophobic interaction or hydrogen bonding were also observed to play a role in the interaction between arginine and Capto MMC, which likely results in the characteristic elution by arginine.
Copyright © 2014 Elsevier B.V. All rights reserved.

Entities:  

Keywords:  Arginine; Free energy; Molecular dynamics simulation; Multimodal chromatography; Polyacrylamide gel electrophoresis

Mesh:

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Year:  2014        PMID: 24642397     DOI: 10.1016/j.chroma.2014.02.053

Source DB:  PubMed          Journal:  J Chromatogr A        ISSN: 0021-9673            Impact factor:   4.759


  1 in total

1.  Rational peptide design for regulating liquid-liquid phase separation on the basis of residue-residue contact energy.

Authors:  Kiyoto Kamagata; Maulana Ariefai; Hiroto Takahashi; Atsumi Hando; Dwiky Rendra Graha Subekti; Keisuke Ikeda; Atsushi Hirano; Tomoshi Kameda
Journal:  Sci Rep       Date:  2022-08-12       Impact factor: 4.996

  1 in total

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