Evidence for a repeating 3,4-dihydroxyphenylalanine- and hydroxyproline-containing decapeptide in the adhesive protein of the mussel, Mytilus edulis L.

Abstract

Previous work has shown that the permanent adhesive of the marine mussel Mytilus edulis is a protein containing large amounts of hydroxyproline (13%) and 3,4-dihydroxyphenylalanine (Dopa, 11%). The protein also known as the polyphenolic protein is produced and stored in the exocrine phenol gland of the mussel and deposited onto marine surfaces by the animal's foot during the formation of new adhesive plaques. The adhesive protein has been purified by a combination of ion exchange on sulfonylpropyl-Sephadex and gel filtration on low surface energy chromatographic media. Polyacrylamide gel electrophoresis of the protein at acidic pH shows it to consist of two components having a molecular weight of about 130,000. Treatment of the protein with clostridial collagenase reduced the molecular weight by less than 10%. The collagenase-resistant fragment contains most or all of the Hyp and Dopa. Trypsin treatment of the polyphenolic protein results in extensive degradation. The major tryptic peptide (80%) contains 10 amino acids including Hyp and Dopa and was shown by sequence analysis to be H2N-Ala-Lys-Pro-Ser-Tyr-Hyp-Hyp-Thr-Dopa-Lys-COOH. Calculations suggest that this and related sequences may be repeated as often as 75 times in the polyphenolic protein.