Fibroblast adhesion onto methyl–silica gradients with and without preadsorbed protein

Abstract

This study was designed to evaluate the interfacial interactions between proteins and cells and a model surface which varied in its surface energy. The adsorption of proteins from single and binary solutions was studied using ellipsometry and the adhesion and spreading of L929 fibroblasts has been quantified using image analysis. The results demonstrated that after 24 h incubation, multilayer adsorbed fibrinogen appeared to produce a surface most conductive to cell adhesion and spreading on both the hydrophilic and hydrophobic regions of the material. Fibronectin on its own did not produce an optimal surface for cell spreading. Albumin produced a suitable surface for cell spreading on the hydrophilic part of the surface, but created a highly unsuitable surface on the hydrophobic region of the specimens. Competition between proteins for adsorption to the surface and changes in protein conformation was evident, particularly on the hydrophobic part of the material, and this was shown to influence cell adhesion and spreading.