Mussel-Glue Derived Peptide–Polymer Conjugates to Realize Enzyme-Activated Antifouling Coatings

P. Wilke and H. G. Börner,

Humboldt Universität zu Berlin; Department of Chemistry; Laboratory for Organic Synthesis of Functional Systems; Brook-Taylor-Str. 2, 12489 Berlin (Germany).

Conjugation of poly(ethylene oxide) (PEO) to a decapeptide that has been derived from a native mussel coat protein results in a functional bioconjugate, which can be enzymatically activated by tyrosinase. A distinct two step oxidation reaction activates the peptide sequence by transforming two Tyr residues into 3,4-dihydroxy-L-phenylalanine derivatives (DOPA-quinone). This up-regulates the adhesive properties of the bioconjugate from reversible weak steel binder to a strong, adhesive to steel substrates as shown by quartz crystal microbalance measurements (QCM). The coating exhibits PEO, which is attached via peptide-mediated non-covalent substrate binding. A significant reduction of protein adsorption (human full blood serum and bovine serum albumin) on the coated substrates revealed potential anti-fouling properties. The stable precursor bioconjugate was not suffering from a lack of stability as the sensitive DOPA-residues were produced in situ, prior to the coating, which paves the way for developments of practical enzyme activated DOPA-quinone glues or coatings.