The interaction of plasma proteins with polymers. I. Relationship between polymer surface energy and protein adsorption/desorption.
Adsorption of bovine albumin, gamma-globulin and fibrinogen from phosphate buffer solution (pH = 7.5) onto several polymer films was studied using the radioiodinated proteins (125I). The kinetics of desorption of the proteinated polymer films in bovine plasma was determined. Contact angle measurements on these same polymers allowed the calculation of dispersive (WA d) and polar (Ip) components of the polymer-protein solution system. Results from these measurements show that the nondispersive-dispersive force balance at the polymer-protein solution interface, expressed by the Ip/WA d ratio, is an important factor for binding of proteins on polymer surfaces. The purity of fibrinogen and the cleaning procedures for the polymer surfaces influence the absolute values of proteins adsorbed on polymer surfaces.
D000327:Adsorption; D000818:Animals; D001672:Biocompatible Materials; D001798:Blood Proteins; D002417:Cattle; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D005340:Fibrinogen; D008956:Models, Chemical; D011108:Polymers; D011138:Polytetrafluoroethylene; D012709:Serum Albumin; D012826:Silicone Elastomers; D013499:Surface Properties; D005719:gamma-Globulins
D001672:Biocompatible Materials; D001798:Blood Proteins; D011108:Polymers; D012709:Serum Albumin; D012826:Silicone Elastomers; D005719:gamma-Globulins; D005340:Fibrinogen; D011138:Polytetrafluoroethylene