Ein Vergleich von Modellen für Interphasenkräfte in Euler‐Euler CFD‐Simulationen von Blasensäulen

Abstract

© 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim Chem. Ing. Tech. 2014, 86, No. 9, 1615–1632 Dye-ligand affinity chromatography is widely utilized for protein separation and purification. Immobilized textile trazine dyes, particularly Cibacron blue, have been applied as affinity chromatography tools for a long time. However, its interaction with a large number of seemingly unrelated proteins inevitably compromises its protein-binding specificity. This endows Cibacron blue with a serious drawback. To cope with the lack of specificity of textile dyes, a better understanding of the binding and specific mechanisms between dye-ligand and different proteins is required. For a detailed investigation into the interaction between Cibacron blue and proteins, molecular dynamics simulations were applied to study the interactions of Cibacron blue with two different proteins, serum albumin and hemoglobin. Allatom models of these affinity interaction systems were employed for a precise study. The interaction as well as the binding sites of proteins are analyzed and discussed in detail. For a better understanding of the specific mechanism, the simulations of these two proteins are compared. The simulation results are combined with the former experimental results to obtain a comprehensive understanding, which is important for the design of new dye-ligands as well as for optimization of dye-ligand affinity chromatography.