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Common blue mussel (Mytilus edulis) is a sessile organism that has unique ability to attach to a wide array of organic and inorganic marine surfaces using its holdfast structures. Strong adhesion to surfaces is essential for mussel survival, movement, and self-defense. Mussel proteins from byssal thread are structural components connecting soft mussel tissues to marine surfaces via an adhesive plaque in the distal end, while adhesive proteins from byssal plaque are responsible for mussel adhesion. Adhesive proteins are small molecules containing a high proportion of post-translationally modified amino acids such as 3,4-dihydroxyphenylalanine (DOPA). High DOPA content, small molecular size, protein flexibility, the presence of metal ions, and a high oxidation state enable strong mussel adhesion to surfaces. Mussel adhesion mechanisms depend on the composition and interactions of mussel proteins, as well as their interactions with the environment. Difficulties in the extraction of mussel adhesion proteins hamper mechanism studies and their practical applications. Development of recombinant mussel proteins and biomimetics will advance our understanding of adhesion mechanisms. In this paper, recent advances in the characterization of mussel adhesive proteins (MAPs), mussel adhesion mechanisms, application of MAPs, and the development of biomimetic biopolymers are reviewed.
Bandara et al. (Fri,) studied this question.