Enzyme-Triggered Antifouling Coatings: Switching Bioconjugate Adsorption via Proteolytically Cleavable Interfering
Maria Meißler1, Andreas Taden2, Hans G Börner1
1Humboldt-Universität zu Berlin, Department of Chemistry, Laboratory for Organic Synthesis of Functional Systems, Brook-Taylor-Str. 2, 12489 Berlin, Germany.
Abstract:
Protease activable antifouling coatings based on peptide-poly(ethylene glycol) conjugates are shown. The material-specific adsorption of a bioconjugate is temporarily suppressed by extending a titanium binding sequence with a proteolytically cleavable epitope and a suitable interfering domain. The adsorption of the PEG-peptide conjugates onto titanium substrates can be regained by cleaving the interfering domain with Tobacco Etch Virus protease. This activates peptide-mediated PEGylation of titanium surfaces and results in coatings that are stable against dilution and suppress nonreversible adsorption of blood protein models. Effects of branched and linear peptidic binding domains on coating stability and antifouling properties are elucidated.
