Cited by 463Polymer Surface Interaction StudiesMarine Biology and Environmental ChemistryBiochemical and Structural Characterization

Mussel protein adhesion depends on interprotein thiol-mediated redox modulation

Open access
Yu, Jing, Wei, Wei, Danner, Eric, Ashley, Rebekah K, Israelachvili, Jacob N, Waite, J Herbert·2011·Nature Chemical Biology

Abstract

Mussel adhesion is mediated by foot proteins (mfps) rich in a catecholic amino acid, 3,4-dihydroxyphenylalanine (dopa), capable of forming strong bidentate interactions with a variety of surfaces. A tendency toward facile auto-oxidation, however, often renders dopa unreliable for adhesion. We demonstrate that mussels limit dopa oxidation during adhesive plaque formation by imposing an acidic, reducing regime based on the thiol-rich mfp-6, which restores dopa by coupling the oxidation of thiols to dopaquinone reduction.

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Crossref · 10.1038/nchembio.630

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1 of 1 references verified0 citation errors · 0 not checkable

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  • The catechol group is prone to oxidation, which may reduce adhesive performance and induce accidental crosslinking.

    “First, the catechol group is prone to oxidation. The oxidation of catechol may reduce the adhesive performance of mussel-inspired hydrogels, especially for some mineral or metal substrates, and is prone to inducing accidental crosslinking [155].”

    From Mussel-Inspired Injectable Adhesive Hydrogels for Biomedical Applications (2024) · cites this paper as [155]

    The opening passage following the Abstract states that dopa readily oxidizes to dopaquinone, diminishing adhesion to titania and mica by at least 80% and making further reactions, including cross-linking, likely. The paper supports the proposed mechanism, but the cited passage does not establish reduced adhesive performance specifically in mussel-inspired hydrogels. (LLM, conf=0.84)

    Experimental — accuracy not yet measured
  • Long-term storage of precursor solutions of mussel-inspired hydrogels is usually difficult.

    “The long-term storage of precursor solutions of mussel-inspired hydrogels is usually difficult.”

    From Mussel-Inspired Injectable Adhesive Hydrogels for Biomedical Applications (2024) · cites this paper as [155]

    The Abstract says dopa readily oxidizes and that this presents challenges for its use in synthetic polymers with dopa-like side chains. It does not address mussel-inspired hydrogel precursor solutions or say that their long-term storage is usually difficult; searches for storage and hydrogel precursors found no such passage. (LLM, conf=0.76)

    Experimental — accuracy not yet measured
  • The thiol group can restore dopa from oxidized dopaquinone, benefiting preservation of catechol groups.

    “The thiol group has been reported to be able to restore dopa from oxidized dopaquinone [155].”

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Cites

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Research works printed but not linked: 21

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Cited by

Sorted by citations

Authors
Yu, J., Wei, W., Danner, E., Ashley, R. K., Israelachvili, J. N., & Waite, J. H.
Affiliations
University of California, Santa Barbara (US)
Venue
Nature Chemical Biology
Published
2011-07-31
Volume
7
Issue
9
Pages
588-590
ISSN
  • 1552-4450 (ISSN-L)
  • 1552-4469
OpenAlex
W1992011929
Cited by
463
References
1
Citations by year
2026: 24 · 2025: 35 · 2024: 31 · 2023: 28 · 2022: 41 · 2021: 33 · 2020: 41 · 2019: 33 · 2018: 30 · 2017: 37 · 2016: 30 · 2015: 22 · 2014: 37 · 2013: 18 · 2012: 20
FWCI
11.53
Type
journal article
Language
en
Open access
Locations
  • Nature Chemical Biology (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
  • eScholarship (California Digital Library) (submittedVersion)
Funders
  • National Science Foundation (R01 DE018468)
  • National Institutes of Health
  • Materials Research Science and Engineering Center, Harvard University
  • National Institute for Materials Science
  • National Institute of Dental and Craniofacial Research (R01DE018468)
Topics
  • Physical Sciences › Materials Science › Surfaces, Coatings and Films › Polymer Surface Interaction Studies
  • Physical Sciences › Engineering › Ocean Engineering › Marine Biology and Environmental Chemistry
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
Keywords
mussel foot proteins, mussel adhesion, DOPA, 3,4-dihydroxyphenylalanine, autoxidation
MeSH terms
Adhesiveness, Amino Acid Sequence, Animals, Dihydroxyphenylalanine, Molecular Sequence Data, Oxidation-Reduction, Proteins, Sulfhydryl Compounds, Benzoquinones, Bivalvia

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