The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Cross-Linking in Adhesive Quinoproteins: Studies with Model Decapeptides
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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“In addition, biomacromolecules, such as proteins, peptides, and DNA, can anchor on the surface of biosubstitutes via the PDA coating layer [50, 57–60].”
From Polydopamine-Assisted Surface Modification for Bone Biosubstitutes (2016) · cites this paper as [57]
Citations
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Mussel-inspired surface chemistry for multifunctional coatings
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Kinetic Stabilization of the α-Synuclein Protofibril by a Dopamine-α-Synuclein Adduct
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Metadata
- 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
- 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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