Investigation of protein binding affinity in multimodal chromatographic systems using a homologous protein library

摘要: A library of cold shock protein B mutant variants was employed to examine differences in binding behavior ion exchange and multimodal chromatography. Single site mutations introduced at charged amino acids on the surface resulted a homologous set with varying charge density distribution. The retention times mutants varied significantly during linear gradient chromatography both systems. majority proteins were more strongly retained cation resin as compared traditional exchanger. Further, elution order different from that obtained Quantitative structure-property relationship models generated using support vector regression technique shown provide good predictions for resin. coarse-grained ligand docking package various interactions between ligands free solution. utilize multiple interaction types achieve stronger surface. use this concert qualitative quantitative analyses presented paper provides an improved understanding chromatographic