Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1999-8-5
pubmed:abstractText
Marine mussels (Mytilus) are experts at bonding to a variety of solid surfaces in a wet, saline and turbulent environment. Bonding is rapid, permanent, versatile and protein-based. In mussels, adhesive bonding takes the form of a byssus--a bundle of extracorporeal threads--each connected to living tissues of the animal at one end and secured by an adhesive plaque at the other. We have investigated the composition and formation of byssal plaques and threads with the hope of discovering technologically relevant innovations in chemistry and materials science. All proteins isolated from the byssus to date share the quality of containing the unusual amino acid, 3,4-dihydroxyphenylalanine. This residue appears to have a dual functionality with significant consequences for adsorption and cohesion. On the one hand, it forms a diverse array of weaker molecular interactions such as metal chelates, H-bonds, and pi-cations: these appear to dominate in surface behavior (adsorption). On the other hand, 3,4-dihydroxyphenylalanine and its redox couple, dopaquinone, can mediate formation of covalent cross-links among byssal proteins (cohesion). One of the challenges in making functional biomimetic versions of byssal adhesion is to understand how these two reactivities are balanced.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0077-8923
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
875
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
301-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Reverse engineering of bioadhesion in marine mussels.
pubmed:affiliation
Marine Biology/Biochemistry Program, University of Delaware, Newark, USA. waite@lifesci.ucsb.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.