Mussel adhesion is mediated by foot proteins (mfps) rich in a catecholic amino acid, 3,4-dihydroxyphenylalanine (dopa), capable of forming strong bidentate interactions with a variety of surfaces. A tendency toward facile auto-oxidation, however, often renders dopa unreliable for adhesion. We demonstrate that mussels limit dopa oxidation during adhesive plaque formation by imposing an acidic, reducing regime based on the thiol-rich mfp-6, which restores dopa by coupling the oxidation of thiols to dopaquinone reduction.
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