Polymerization of Quinone-Crosslinked Marine Bioadhesive Protein

Abstract

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.

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Document Details

Document Type
Technical Report
Publication Date
Oct 05, 1988
Accession Number
ADA200224

Entities

People

  • J. H. Waite

Organizations

  • University of Delaware

Tags

Communities of Interest

  • Materials and Manufacturing Processes

DTIC Thesaurus Topics

  • Acquisition
  • Addition Reactions
  • Adhesives
  • Amines
  • Amino Acids
  • Analogs
  • Cells
  • Composite Materials
  • Contracts
  • Delaware
  • Hydrophobic Properties
  • Military Research
  • Oxidation
  • Polymerization
  • Sequences
  • Side Reactions
  • Universities

Fields of Study

  • Biology
  • Chemistry

Readers

  • Molecular and Cellular Biochemistry