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pubmed:abstractText |
The byssus of marine mussels has attracted attention as a paradigm of strong and versatile underwater adhesion. As the first of the 3,4-dihydroxyphenylalanine (Dopa)-containing byssal precursors to be purified, Mytilus edulis foot protein-1 (mefp-1) has been much investigated with respect to its molecular structure, physical properties, and adsorption to surfaces. Although mefp-1 undoubtedly contributes to the durability of byssus, it is not directly involved in adhesion. Rather, it provides a robust coating that is 4-5 times stiffer and harder than the byssal collagens that it covers. Protective coatings for compliant tissues and materials are highly appealing to technology, notwithstanding the conventional wisdom that coating extensibility can be increased only at the expense of hardness and stiffness. The byssal cuticle is the only known coating in which high compliance and hardness co-exist without mutual detriment; thus, the role of mefp-1 in accommodating both parameters deserves further study.
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