Enzyme-triggered antifouling coatings: switching bioconjugate adsorption via proteolytically cleavable interfering domains.

Maria Meißler, Andreas Taden, and Hans G. Börner

doi: 10.1021/acsmacrolett.6b00072


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.