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Metals and the integrity of a biological coating: The cuticle of mussel byssus
University of California at Santa Barbara, Chemistry Department.ORCID iD: 0000-0001-5678-5298
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2009 (English)In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 25, no 6, p. 3323-3326Article in journal (Refereed) Published
Abstract [en]

The cuticle of mussel byssal threads is a robust natural coating that combines high extensibility with high stiffness and hardness. In this study, fluorescence microscopy and elemental analysis were exploited to show that the 3,4-dihydroxyphenyl-L-alanine (dopa) residues of mussel foot protein-1 colocalize with Fe and Ca distributions in the cuticle of Mytilus galloprovincialis mussel byssal threads. Chelated removal of Fe and Ca from the cuticle of intact threads resulted in a 50% reduction in cuticle hardness, and thin sections subjected to the same treatment showed a disruption of cuticle integrity. Dopa-metal complexes may provide significant interactions for the integrity of composite cuticles deformed under tension.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2009. Vol. 25, no 6, p. 3323-3326
Keyword [en]
CROSS-LINKING; HYBRID COATINGS; EIMERIA-MAXIMA; MYTILUS-EDULIS; OOCYST WALL; ADHESIVE; PROTEINS; MECHANICS; PRECURSOR; OXIDATION
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:kth:diva-86776DOI: 10.1021/la8027012ISI: 000264145000001OAI: oai:DiVA.org:kth-86776DiVA, id: diva2:502725
Note
cited By (since 1996) 23 QC 20120216Available from: 2012-02-16 Created: 2012-02-13 Last updated: 2017-12-07Bibliographically approved

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Toprak,, M.S.

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