The range and potential contribution of irreversibly adsorbed proteins on the surface of artificial implants

Abstract

Protein adsorption is the first stage of the interaction between prosthetic materials with tissues of the body. They undergo conformational changes depending on the chemical composition and the nanotopography surface. Adsorbed proteins induce adhesion and alter the functional state of migrating cells. Plasma samples from patients were incubated with such matrices as titanium, polypropylene or polyester with fluoropolymer coating meshes. Bound peptides were analyzed by electrophoresis. Qualitative analysis of the peptides extracted from the gel was performed by chromatography-mass spectrometry. Quantitative analysis was performed by the MRM method. More than 60 proteins were identified on the analyzed surfaces. Quantitative analysis showed preferential adsorption of vitronectin, albumin, fibrinogen a-chain, C1ѕ component of the complement system. Vitronectin had the maximum relative protein content. Since biocompatibility of the analyzed materials varies considerably this variability may be attributed to conformational changes occurring with vitronectin during its irreversible adsorption.