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The glue protein of ribbed mussels (Geukensia demissa): a natural adhesive with some features of collagen

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The Atlantic ribbed musselGeukensia (Modiolus)demissa attaches itself to the roots of cord grass and other hard objects in tidal salt marshes by spinning adhesive byssal threads. The precursor of a protein apparently present in the adhesive plaques of the threads was isolated in quantity from the foot of the mussel. The protein has an apparent molecular weight of 130000, a pI of 8.1, and contains a high proportion of Gly, Glu/Gln, Lys and 3,4-dihydroxyphenyl-l-alanine (DOPA). Sequence of tryptic peptides suggests a pattern of repeated motifs, such as: Gly-DOPA-Lys, and X-Gly-DOPA-Y-Z-Gly-DOPA/Tyr-Lys, where X is Thr or Ala in octapeptides and Gln-Thr in nonapeptides. Y is variable, but more often than not hydrophobic; and Z is frequently Pro or 4-trans-hydroxyproline (Hyp). The presence of Pro-Gly and Hyp-Gly sequences of δ-hydroxylysine in the protein is reminiscent of typical collagens; however, the protein is not labile to clostridial collagenase, nor does collagen cross-react with antibodies raised against the mussel protein. Unlike typical collagens, Gly probably occurs only at every 4th or 5th residue in this unusual mussel protein.

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Anti-Gdfp :

anti-G. demissa foot protein

Dopa :



cetyltrimethylammonium bromide


high performance liquid chromatography


polyacrylamide gel electrophoresis


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Correspondence to J. Herbert Waite.

Additional information

Supported by grants from the National Science Foundation (DMB 8500301) and the Office of Naval Research (N00014-86K-0717)

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Waite, J.H., Hansen, D.C. & Little, K.T. The glue protein of ribbed mussels (Geukensia demissa): a natural adhesive with some features of collagen. J Comp Physiol B 159, 517–525 (1989). https://doi.org/10.1007/BF00694376

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Key words

  • Byssus
  • DOPA
  • Glue Protein
  • Mussel