PH-dependent cross-linking of catechols through oxidation via Fe³⁺ and potential implications for mussel adhesion.

ABSTRACT: The mussel byssus is a remarkable attachment structure that is formed by injection molding and rapid in-situ hardening of concentrated solutions of proteins enriched in the catecholic amino acid 3,4-dihydroxy-L-phenylalanine (DOPA). Fe³⁺, found in high concentrations in the byssus, has been speculated to participate in redox reactions with DOPA that lead to protein polymerization, however direct evidence to support this hypothesis has been lacking. Using small molecule catechols, DOPA-containing peptides, and native mussel foot proteins, we report the first direct observation of catechol oxidation and polymerization accompanied by reduction of Fe³⁺ to Fe²⁺. In the case of the small molecule catechol, we identified two dominant dimer species and characterize

SUBMITTER: Fullenkamp DE 

PROVIDER: S-EPMC4164901 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature