贻贝类蛋白质黏附取决于蛋白间巯基介导的氧化还原调节。

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

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.

贻贝的黏附是由富含儿茶酚氨基酸（3,4-二羟基苯丙氨酸，即 DOPA）的足部蛋白（mfps）介导的，这种氨基酸能够与各种表面形成强双配位相互作用。然而，DOPA 极易自动氧化，因此通常使其在黏附斑块形成过程中变得不可靠。我们证明，贻贝通过富含巯基的 mf p-6 施加酸性还原环境来限制黏附斑形成过程中的 DOPA 氧化，通过将巯基的氧化与 DOPA 醌的还原偶联来恢复 DOPA。