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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Adhesiveness
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Amino Acid Sequence
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Animals
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Benzoquinones / chemistry
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Bivalvia / physiology
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Dihydroxyphenylalanine / analogs & derivatives
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Dihydroxyphenylalanine / chemistry*
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Molecular Sequence Data
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Oxidation-Reduction
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Proteins / chemistry*
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Sulfhydryl Compounds / chemistry*
Substances
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Benzoquinones
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Proteins
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Sulfhydryl Compounds
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adhesive protein, mussel
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Dihydroxyphenylalanine
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dopaquinone