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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, 3323-3326 p.Article 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, 3323-3326 p.
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: 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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