Mussel protein adhesion depends on interprotein thiol-mediated redox modulation

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


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

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Adhesiveness
  • Amino Acid Sequence
  • Animals
  • Benzoquinones / chemistry
  • Bivalvia / physiology
  • Dihydroxyphenylalanine / analogs & derivatives
  • Dihydroxyphenylalanine / chemistry*
  • Molecular Sequence Data
  • Oxidation-Reduction
  • Proteins / chemistry*
  • Sulfhydryl Compounds / chemistry*


  • Benzoquinones
  • Proteins
  • Sulfhydryl Compounds
  • adhesive protein, mussel
  • Dihydroxyphenylalanine
  • dopaquinone