Characterization of plasmatic proteins adsorption on poly(styrene sodium sulfonate) functionalized silicone surfaces.

Proteins adsorption occurs spontaneously on biomaterial upon insertion within the body. The resulting protein layer influences biomaterial biocompatibility through enhanced bio-integration or, on the contrary, adverse reactions. Furthermore, upon adsorption, proteins can undergo modifications of their structure and, ultimately, their physicochemical properties and activity. Hence, the understanding of protein adsorption on implanted materials appears essential, as exemplified by silicone breast prostheses that might lead to serious health issues. Surface modifications with a bioactive polymer, poly(styrene sodium sulfonate)-polyNaSS, on a hydrophobic silicone surface that composes breast implants, have been successfully performed under UV irradiation by a radical surface polymerization. This strategy enhances cell biocompatibility and antibacterial features. Although detailed insights related to the mechanism are still scarce, polyNaSS is supposed to promote changes in the conformation and/or orientation of adsorbed plasma proteins, reducing the odd for a biofilm to form. The present work addresses more in-depth structural investigations of the adsorbed state of two plasma proteins: Bovine Serum Albumin (BSA), as a model protein, and fibronectin (FN), for its role in cell adhesion. Using Atomic force microscopy (AFM), we report that polyNaSS showed no significant impact on the BSA structure conversely to the FN one. However, imaging findings with AFM clearly outlined a change in the structural organization of FN, going from a nano fibrillar assembly with an average length of 130 nm to a globular one when the surface was grafted. Thus, it is highlighted that polyNaSS interacts specifically with FN. In addition, cell spreading assay of L929 fibroblasts on FN-coated surfaces with optical microscopy indicated no significant impact of the change in FN structure upon fibroblasts adhesion, which displayed active elongated shapes. The present features are crucial for understanding the cell adhesion mechanism induced by surface modification.