| Literature DB >> 18847291 |
Niels Holten-Andersen1, Thomas E Mates, Muhammet S Toprak, Galen D Stucky, Frank W Zok, J Herbert Waite.
Abstract
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.Entities:
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Year: 2009 PMID： 18847291 PMCID： PMC2746015 DOI： 10.1021/la8027012
Source DB: PubMed Journal: Langmuir ISSN： 0743-7463 Impact factor: 3.882