title: 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.
authors.affiliation: Department of Chemical Engineering, University of California, Santa Barbara, Santa Barbara, California, USA.
authors.forename: Jing
authors.initials: J
authors.lastname: Yu
authors.forename: Wei
authors.initials: W
authors.lastname: Wei
authors.forename: Eric
authors.initials: E
authors.lastname: Danner
authors.forename: Rebekah K
authors.initials: RK
authors.lastname: Ashley
authors.forename: Jacob N
authors.initials: JN
authors.lastname: Israelachvili
authors.forename: J Herbert
authors.initials: JH
authors.lastname: Waite
mesh_terms: D000268:Adhesiveness; D000595:Amino Acid Sequence; D000818:Animals; D016227:Benzoquinones / Q000737:chemistry; D049872:Bivalvia / Q000502:physiology; D004295:Dihydroxyphenylalanine / Q000031:analogs & derivatives / Q000737:chemistry*; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D011506:Proteins / Q000737:chemistry*; D013438:Sulfhydryl Compounds / Q000737:chemistry*
chemical_list: D016227:Benzoquinones; D011506:Proteins; D013438:Sulfhydryl Compounds; C037403:adhesive protein, mussel; D004295:Dihydroxyphenylalanine; C035157:dopaquinone