Correlation between protein desorption behavior and its adsorption enthalpy change in polymer grafted anion exchange chromatography
نویسندگان
چکیده
Thermodynamic studies on protein adsorption onto chromatographic surfaces mainly focus the molecular level interaction between proteins and ligands. Yet, not much attention is given to study of polymer grafted ligand architecture effect thermodynamic parameters, nor relation parameters directly obtained parameters. These relations are needed in order confer meaning ease future data interpretation adsorption. In this study, bovine serum albumin monomer (BSAm) with ligands was studied from a point view together data. Isothermal titration calorimetry (ITC) results showed that BSAm exothermic (ΔH¯ads < 0) when adsorbs Toyopearl GigaCapQ 650 M, Q600AR, Q Sepharose XL, but endothermic > SuperQ conventional resin (Q Fast Flow), showing clear differences driving forces caused by different architectures. addition, we found new salt required for elution change enthalpy (ΔH¯ads) measured ITC, intrinsically connecting both desorption mechanisms.
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ژورنال
عنوان ژورنال: Colloids and Surfaces B: Biointerfaces
سال: 2021
ISSN: ['0927-7765', '1873-4367']
DOI: https://doi.org/10.1016/j.colsurfb.2021.111853