McQueen-Quattlebaum Professor Department of Bioengineering, Clemson University, Clemson, SC, United States.
Colloids Surf B Biointerfaces. 2020 Jul;191:110992. doi: 10.1016/j.colsurfb.2020.110992. Epub 2020 Apr 1.
Protein adsorption is important for essentially any process that involves the contact of a protein-containing solution and a material surface, with the resulting formation of the adsorbed layer of protein determined by the thermodynamics and kinetics of the system involved. This paper presents an overview of the fundamentals of these processes. First, the hierarchical structure of proteins and the types of bonding that stabilize a protein's native-state structure are presented. This section is then followed by a section presenting the thermodynamic driving forces that influence the way that proteins adsorb and conformationally change for three characteristically different types of surface chemistries: nonpolar (hydrophobic) surfaces, neutral hydrophilic surfaces, and charged surfaces. The final section of this paper addresses how kinetics and thermodynamics combine together to influence protein adsorption behavior, followed by concluding remarks.
蛋白质吸附对于任何涉及含有蛋白质的溶液与材料表面接触的过程都很重要，所形成的蛋白质吸附层取决于所涉及的系统的热力学和动力学。本文概述了这些过程的基本原理。首先介绍了蛋白质的层次结构和稳定蛋白质天然结构的键的类型。然后介绍了影响蛋白质吸附和构象变化的热力学驱动力，这些驱动力适用于三种具有显著不同特性的表面化学物质：非极性（疏水）表面、中性亲水表面和带电表面。本文的最后一部分讨论了动力学和热力学如何结合起来影响蛋白质吸附行为，最后是结论。
