Journal
SCIENCE
Volume 328, Issue 5975, Pages 216-220Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1181044
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Funding
- Alexander von Humboldt Foundation
- Federal Ministry of Education and Research
- NIH [R01DE018468]
- Danish Natural Science Research Council [272-08-0087]
- Materials Research and Engineering Center Program of NSF [DMR05-20415]
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The extensible byssal threads of marine mussels are shielded from abrasion in wave-swept habitats by an outer cuticle that is largely proteinaceous and approximately fivefold harder than the thread core. Threads from several species exhibit granular cuticles containing a protein that is rich in the catecholic amino acid 3,4-dihydroxyphenylalanine (dopa) as well as inorganic ions, notably Fe3+. Granular cuticles exhibit a remarkable combination of high hardness and high extensibility. We explored byssus cuticle chemistry by means of in situ resonance Raman spectroscopy and demonstrated that the cuticle is a polymeric scaffold stabilized by catecholato-iron chelate complexes having an unusual clustered distribution. Consistent with byssal cuticle chemistry and mechanics, we present a model in which dense cross-linking in the granules provides hardness, whereas the less cross-linked matrix provides extensibility.
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