Cited by 485Polymer Surface Interaction StudiesBiochemical and Structural CharacterizationMarine Biology and Environmental Chemistry

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Cross-Linking in Adhesive Quinoproteins: Studies with Model Decapeptides

Burzio, Luis A., Waite, J. Herbert·2000·Biochemistry

DOI 10.1021/bi0002434

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Abstract

Mytilus edulis foot protein-1 (mefp1) is a major component of the byssus, an adhesive holdfast in mussels. The recent report of 5, 5'-di(dihydroxyphenyl-L-alanine) (diDOPA) cross-links in byssus [McDowell et al. (1999) J. Biol. Chem. 274, 20293] has raised questions about the relationship of these to mefp1. About 80% of the primary structure of mefp1 consists of a tandemly repeated consensus sequence Ala(1)-Lys(2)-Pro(3)-Ser(4)-Tyr(5)-Pro(6)-Pro(7)-Thr(8)-Tyr(9)-Lys(10 ) with varying degrees of posttranslational hydroxylation to hydroxyprolines in positions 3, 6, and 7 and to DOPA in positions 5 and 9. Six natural or synthetic variants of this decapeptide were subjected to oxidation by tyrosinase or periodate. DOPA is the only residue to suffer losses in all oxidized peptides. Moreover, using MALDI TOF mass spectrometry, oxidized decapeptides all showed evidence of multimer formation and a mass loss of 6 Da per coupled pair of peptides. Multimer formation was inhibited by addition of DOPA-like o-diphenols, but addition of simple amines such as free Lys had no effect. The results are consistent with aryloxy coupling to diDOPA followed by reoxidation to diDOPA quinone. There are subtle but noteworthy variations, however, in multimer formation among the peptide congeners. Decapeptides with Pro(3) modified to trans-4-hydroxyproline do not form multimers beyond dimers; they also exhibit significant Lys losses following oxidation of DOPA. Moreover, in Ala-Lys-Hyp-Ser-Tyr-DiHyp-Hyp-…

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Self-citation

Authors: Burzio, L. A., & Waite, J. H.
Affiliations: University of California, Santa Barbara (US)
ORCID: Waite, J. Herbert
Venue: Biochemistry
Publisher: American Chemical Society (ACS)
Published: 2000-08-17
Volume: 39
Issue: 36
Pages: 11147-11153
ISSN: 0006-2960 (ISSN-L)
1520-4995
DOI: 10.1021/bi0002434
OpenAlex: W2011121154
Cited by: 485
References: 9
Citations by year: 2026: 4 · 2025: 9 · 2024: 18 · 2023: 19 · 2022: 23 · 2021: 37 · 2020: 25 · 2019: 29 · 2018: 28 · 2017: 34 · 2016: 37 · 2015: 24 · 2014: 28 · 2013: 19 · 2012: 24
FWCI: 6.45
Type: journal article
Language: en
Open access: closed
Locations: Biochemistry (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r01de010042-11)
National Institute of Dental and Craniofacial Research (DE10042)
Topics: Physical Sciences › Materials Science › Surfaces, Coatings and Films › Polymer Surface Interaction Studies
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
Physical Sciences › Engineering › Ocean Engineering › Marine Biology and Environmental Chemistry
Keywords: byssus, DOPA oxidation, periodate oxidation, hydroxyproline, trans-4-hydroxyproline, o-diphenols
MeSH terms: Adhesiveness, Adhesives, Animals, Cross-Linking Reagents, Dihydroxyphenylalanine, Glycine, Hydrolysis, Lysine, Models, Molecular, Oligopeptides, Oxidation-Reduction, Proteins, Quinones, Spectrophotometry, Ultraviolet, Tyrosine, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Bivalvia

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Cross-Linking in Adhesive Quinoproteins: Studies with Model Decapeptides

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