Journal
LANGMUIR
Volume 25, Issue 6, Pages 3323-3326Publisher
AMER CHEMICAL SOC
DOI: 10.1021/la8027012
Keywords
-
Funding
- National Institutes of Health [R0I DE015415, R01GM65354]
- National Science Foundation [DMR00-80034]
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available