Metals and the Integrity of a Biological Coating: The Cuticle of Mussel Byssus

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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.
Publisher
AMER CHEMICAL SOC
Issue Date
2009-03
Language
English
Article Type
Article
Keywords

CROSS-LINKING; HYBRID COATINGS; EIMERIA-MAXIMA; MYTILUS-EDULIS; OOCYST WALL; ADHESIVE; PROTEINS; MECHANICS; PRECURSOR; OXIDATION

Citation

LANGMUIR, v.25, no.6, pp.3323 - 3326

ISSN
0743-7463
DOI
10.1021/la8027012
URI
http://hdl.handle.net/10203/93805
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