Distinct adsorption configurations and self-assembly characteristics of fibrinogen on chemically uniform and alternating surfaces including block copolymer nanodomains.

ABSTRACT: Understanding protein-surface interactions is crucial to solid-state biomedical applications whose functionality is directly correlated with the precise control of the adsorption configuration, surface packing, loading density, and bioactivity of protein molecules. Because of the small dimensions and highly amphiphilic nature of proteins, investigation of protein adsorption performed on nanoscale topology can shed light on subprotein-level interaction preferences. In this study, we examine the adsorption and assembly behavior of a highly elongated protein, fibrinogen, on both chemically uniform (as-is and buffered HF-treated SiO2/Si, and homopolymers of polystyrene and poly(methyl methacrylate)) and varying (polystyrene-block-poly(methyl methacrylate)) surfaces. By focusing on high-resolut

SUBMITTER: Song S 

PROVIDER: S-EPMC4046797 | biostudies-literature | 2014 May

REPOSITORIES: biostudies-literature