α,β-Dehydro-Dopa: A Hidden Participant in Mussel Adhesion.

Titleα,β-Dehydro-Dopa: A Hidden Participant in Mussel Adhesion.
Publication TypeJournal Article
Year of Publication2016
AuthorsMirshafian, R, Wei, W, Israelachvili, JN, Waite, JH
JournalBiochemistry
Volume55
Issue5
Pagination743-50
Date Published2016 Feb 9
ISSN1520-4995
Abstract

Dopa (l-3,4-dihydroxyphenylalanine) is a key chemical signature of mussel adhesive proteins, but its susceptibility to oxidation has limited mechanistic investigations as well as practical translation to wet adhesion technology. To investigate peptidyl-Dopa oxidation, the highly diverse chemical environment of Dopa in mussel adhesive proteins was simplified to a peptidyl-Dopa analogue, N-acetyl-Dopa ethyl ester. On the basis of cyclic voltammetry and UV-vis spectroscopy, the Dopa oxidation product at neutral to alkaline pH was shown to be α,β-dehydro-Dopa (ΔD), a vinylcatecholic tautomer of Dopa-quinone. ΔD exhibited an adsorption capacity on TiO2 20-fold higher than that of the Dopa homologue in the quartz crystal microbalance. Cyclic voltammetry confirmed the spontaneity of ΔD formation in mussel foot protein 3F at neutral pH that is coupled to a change in protein secondary structure from random coil to β-sheet. A more complete characterization of ΔD reactivity adds a significant new perspective to mussel adhesive chemistry and the design of synthetic bioinspired adhesives.

DOI10.1021/acs.biochem.5b01177
Alternate JournalBiochemistry
PubMed ID26745013
PubMed Central IDPMC4760353
Grant ListR01 DE018468 / DE / NIDCR NIH HHS / United States