Mussel protein adhesion depends on interprotein thiol-mediated redox modulation.

ABSTRACT: 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.

SUBMITTER: Yu J 

PROVIDER: S-EPMC3158268 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature