Protein adsorption on polymeric biomaterials I. Adsorption isotherms

• Published in: Journal of colloid and interface science Vol. 124; no. 1; pp. 28 - 43
• Main Authors: Young, B.R, Pitt, W.G, Cooper, S.L
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 01.07.1988; Elsevier
• Subjects: Biological and medical sciences; Fundamental and applied biological sciences. Psychology; Molecular biophysics; Physico-chemical properties of biomolecules; Proteins; Adsorption; Fibrinogen; IgG; Surface properties; Polymer; Biomaterial; Serum albumin
• ISSN: 0021-9797; 1095-7103
• DOI: 10.1016/0021-9797(88)90321-9

the equilibrium adsorption of seven purified human proteins to four different biomaterials was studied at different protein concentraitons under in vitro conditions. The proteins studied were albumin, transferrin, three monoclonal antibodies of different net charge, fibrinogen, and α 2-macroglobulin. The biomaterials used in the adsorption studies included a polyether urethane urea, polyethylene, silicone rubber, and plasticized polyvinyl chloride. The equilibrium adsorption data for these protein-biomaterial combinations could be fit by a protein adsorption model assuming two or more adsorbed protein layers. The monolayer concentrations of adsorbed protein agreed closely with the theoretical monolayer concentrations based on the macromolecular dimensions of the proteins. Protein binding constants decreased for protein layers further away from the surface, and, for the series of biomaterials, protein binding constants decreased with decreasing biomaterial surface-water free energy. From these studies, it is apparent that the magnitude of the binding forces at the liquid-polymer interface is a function of both the biomaterial composition and the individual protein.