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Nat Chem Biol. 2011 Jul 31;7(9):588-90. doi: 10.1038/nchembio.630.

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

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1
Department of Chemical Engineering, University of California, Santa Barbara, Santa Barbara, California, USA.

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.

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PMID:
21804534
PMCID:
PMC3158268
DOI:
10.1038/nchembio.630
[Indexed for MEDLINE]
Free PMC Article
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