Fundamental Principles of the Thermodynamics and Kinetics of Protein Adsorption to Material Surfaces

• Published in: Colloids and surfaces, B, Biointerfaces B, Biointerfaces, 2020-07, Vol.191, p.110992-110992, Article 110992
• Main Author: Latour, Robert A.
• Format: Article
• Language: English
• Subjects: Adsorption; Animals; Humans; Hydrophobic and Hydrophilic Interactions; Kinetics; Protein adsorption; Proteins - chemistry; Proteins - metabolism; Surface Properties; Thermodynamics
• ISSN: 0927-7765; 1873-4367
• DOI: 10.1016/j.colsurfb.2020.110992

[Display omitted] •Fundamental principles governing thermodynamics of protein adsorption.•Fundamental principles governing kinetics of protein adsorption.•Free energy of protein adsorption on nonpolar, polar, and charged surfaces.•Influence of hydration effects on protein adsorption to materials surface.•Influence of ion-exchange on protein adsorption to charged material surfaces. 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.