Numerous strategies exist to prevent biological fouling of surfaces in physiological environments; the authors' strategy focuses on the modification of surfaces with poly-N-substituted glycine oligomers (polypeptoids). The authors previously reported the synthesis and characterization of three novel polypeptoid polymers that can be used to modify titanium oxide surfaces, rendering the surfaces resistant to adsorption of proteins, to adhesion of mammalian and bacterial cells, and to degradation by common protease enzymes. In this study, they investigated the effect of polypeptoid chain length on the antifouling properties of the modified surfaces. For these experiments, they used poly(N-methoxyethyl) glycines with lengths between 10 and 50 repeat units and determined the influence of chain length on coating thickness and density as well as resistance to protein adsorption and cellular adhesion. Short-term protein resistance remained low for all polymers, as measured by optical waveguide light mode spectroscopy, while fibroblast adhesion after several weeks indicated reduced fouling resistance for the polypeptoid-modified surfaces with the shortest chain length polymer. Experimental observations were compared to predictions obtained from a molecular theory of polymer and protein adsorption. Good agreement was found between experiment and theory for the chain length dependence of peptoid grafting density and for protein adsorption as a function of peptoid grafting density. The theoretical predictions provide specific guidelines for the surface coverage for each molecular weight for optimal antifouling. The predictions show the relationship between polymer layer structure and fouling.
|Original language||English (US)|
|State||Published - Jun 2009|
ASJC Scopus subject areas
- Materials Science(all)
- Biochemistry, Genetics and Molecular Biology(all)
- Physics and Astronomy(all)