Ontology highlight
ABSTRACT:
SUBMITTER: Yu J
PROVIDER: S-EPMC3158268 | biostudies-literature | 2011 Jul
REPOSITORIES: biostudies-literature
Yu Jing J Wei Wei W Danner Eric E Ashley Rebekah K RK Israelachvili Jacob N JN Waite J Herbert JH
Nature chemical biology 20110731 9
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 t ...[more]