Polymerization of Quinone-Crosslinked Marine Bioadhesive Protein
DELAWARE UNIV NEWARK COLLEGE OF EARTH OCEAN AND ENVIRONMENT (CEOE)
Pagination or Media Count:
The marine adhesive proteins of some six different invertebrates have been isolated and partially sequenced. These proteins are characterized by having high isoelectric points and high levels of lysine and Dopa. There are few unifying features in the primary sequence. All of the proteins have repeat sequences with consensus peptides ranging from 4 to 10 amino acids. Most of these have C-terminal lysine and Dopa flanked on at least one side by glycine. The cross-linking of these proteins is mediated by catecholoxidase. This enzyme catalyzes the conversion of Dopa to o-quinone. The latter tautomerizes to Alpha, Beta-dehydro-functional groups that are again oxidized by the enzyme, this time to Alpha, Beta-dehydro Dopaquinone. The latter is expected to undergo a diverse assortment of nucleophilic addition reactions.
- Organic Chemistry