期刊
LANGMUIR
卷 25, 期 6, 页码 3323-3326出版社
AMER CHEMICAL SOC
DOI: 10.1021/la8027012
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资金
- National Institutes of Health [R0I DE015415, R01GM65354]
- National Science Foundation [DMR00-80034]
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.
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