Mussel adhesion - essential footwork.

TitleMussel adhesion - essential footwork.
Publication TypeJournal Article
Year of Publication2017
AuthorsJ Waite, H
JournalJ Exp Biol
IssuePt 4
Date Published2017 02 15
KeywordsAdhesiveness, Adhesives, Amino Acid Sequence, Animals, Bivalvia, Dihydroxyphenylalanine, Hydrogen-Ion Concentration, Osmolar Concentration, Proteins, Tensile Strength, Wettability

Robust adhesion to wet, salt-encrusted, corroded and slimy surfaces has been an essential adaptation in the life histories of sessile marine organisms for hundreds of millions of years, but it remains a major impasse for technology. Mussel adhesion has served as one of many model systems providing a fundamental understanding of what is required for attachment to wet surfaces. Most polymer engineers have focused on the use of 3,4-dihydroxyphenyl-l-alanine (Dopa), a peculiar but abundant catecholic amino acid in mussel adhesive proteins. The premise of this Review is that although Dopa does have the potential for diverse cohesive and adhesive interactions, these will be difficult to achieve in synthetic homologs without a deeper knowledge of mussel biology; that is, how, at different length and time scales, mussels regulate the reactivity of their adhesive proteins. To deposit adhesive proteins onto target surfaces, the mussel foot creates an insulated reaction chamber with extreme reaction conditions such as low pH, low ionic strength and high reducing poise. These conditions enable adhesive proteins to undergo controlled fluid-fluid phase separation, surface adsorption and spreading, microstructure formation and, finally, solidification.

Alternate JournalJ. Exp. Biol.
PubMed ID28202646
PubMed Central IDPMC5312731
Grant ListR01 DE018468 / DE / NIDCR NIH HHS / United States