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Peptide repeats in a mussel glue protein: theme and variations

Waite, J. Herbert, Housley, Timothy J., Tanzer, Marvin L.·1985·Biochemistry

Abstract

The adhesive protein from Mytilus edulis contains 75-80 closely related, repeated peptide sequences in its primary structure. These peptides can be resolved following digestion with trypsin by reversed-phase high-pressure liquid chromatography. The most frequently repeated sequence is the decapeptide Ala-Lys-Pro-Ser-Tyr-Hyp-Hyp-Thr-Dopa-Lys (peptide E). Variations of this occur in peptides B with Hyp-3 and Dopa-5, C with Dopa-5, and D with Hyp-3, respectively. Lesser amounts of hexapeptides (A and B') that are lacking residues 4-7 also occur. Peptide A has the sequence Ala-Lys-Pro-Thr-Dopa-Lys, whereas B' contains Tyr instead of Dopa. 4-Hydroxyproline occurs at positions 3 and 7 and occasionally at position 6 of the decapeptide; 3-hydroxyproline occurs only at position 6. Adhesiveness of the protein may be related to the repetition of Dopa residues, the catecholic moiety of which has strong hydrogen-bonding and metal-liganding capabilities.

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Metadata

Authors
Waite, J. H., Housley, T. J., & Tanzer, M. L.
Venue
Biochemistry
Published
1985-09
Volume
24
Issue
19
Pages
5010-5014
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
OpenAlex
W2079897195
Cited by
208
References
0
FWCI
3.48
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Peptide repeats in a mussel glue protein: theme and variations. https://app.cochat.ai/papers/10.1021/bi00340a008
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Waite, J. H., Housley, T. J., & Tanzer, M. L. (1985). Peptide repeats in a mussel glue protein: theme and variations. Biochemistry. https://doi.org/10.1021/bi00340a008

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