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Cited by 2,112Polymer Surface Interaction StudiesMarine Biology and Environmental ChemistryAdhesion, Friction, and Surface Interactions

Single-molecule mechanics of mussel adhesion

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Lee, Haeshin, Scherer, Norbert F., Messersmith, Phillip B.·2006·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.0605552103PMC PMC1559742
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Abstract

The glue proteins secreted by marine mussels bind strongly to virtually all inorganic and organic surfaces in aqueous environments in which most adhesives function poorly. Studies of these functionally unique proteins have revealed the presence of the unusual amino acid 3,4-dihydroxy- l -phenylalanine (dopa), which is formed by posttranslational modification of tyrosine. However, the detailed binding mechanisms of dopa remain unknown, and the chemical basis for mussels’ ability to adhere to both inorganic and organic surfaces has never been fully explained. Herein, we report a single-molecule study of the substrate and oxidation-dependent adhesive properties of dopa. Atomic force microscopy (AFM) measurements of a single dopa residue contacting a wet metal oxide surface reveal a surprisingly high strength yet fully reversible, noncovalent interaction. The magnitude of the bond dissociation energy as well as the inability to observe this interaction with tyrosine suggests that dopa is critical to adhesion and that the binding mechanism is not hydrogen bond formation. Oxidation of dopa, as occurs during curing of the secreted mussel glue, dramatically reduces the strength of the interaction to metal oxide but results in high strength irreversible covalent bond formation to an organic surface. A new picture of the interfacial adhesive role of dopa emerges from these studies, in which dopa exploits a remarkable combination of high strength and chemical multifunctionality to accomplish adhesion to substrates of widely varying composition from organic to metallic.

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  • Coordination bonding and strong chelating bonding with transition metal compounds occur between catechol or diketone groups on the polydopamine coating layer and the interface of inorganic biosubstitutes, along with protein cross-linking.

    “Such coordination bonding and strong chelating bonding with transition metal compound occur between catechol or diketone groups on the PDA coating layer and the interface of inorganic biosubstitutes along with the protein cross-linking [61–66].”

    From Polydopamine-Assisted Surface Modification for Bone Biosubstitutes (2016) · cites this paper as [63]

    The Results and Discussion (page not provided) report strong, reversible coordination bonds between unoxidized dopa and inorganic oxide surfaces, and describe oxidized dopa as participating in protein cross-linking. The paper studies individual dopa residues, not a polydopamine coating on inorganic biosubstitutes; it does not establish the claimed diketone-mediated chelation at that interface. (LLM, conf=0.88)

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Cited by

Sorted by citations

Authors
Lee, H., Scherer, N. F., & Messersmith, P. B.
Affiliations
  • Northwestern University (US)
  • University of Chicago (US)
ORCID
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
2006-08-29
Volume
103
Issue
35
Pages
12999-13003
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.0605552103
PMC
PMC1559742
OpenAlex
W2154577831
Cited by
2,112
References
1
Citations by year
2026: 58 · 2025: 105 · 2024: 102 · 2023: 117 · 2022: 111 · 2021: 152 · 2020: 164 · 2019: 150 · 2018: 149 · 2017: 138 · 2016: 150 · 2015: 114 · 2014: 137 · 2013: 112 · 2012: 108
FWCI
19.39
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Institute of Dental and Craniofacial Research (R01DE014193, DE14193, R37DE014193)
Topics
  • Physical Sciences › Materials Science › Surfaces, Coatings and Films › Polymer Surface Interaction Studies
  • Physical Sciences › Engineering › Ocean Engineering › Marine Biology and Environmental Chemistry
  • Physical Sciences › Engineering › Mechanics of Materials › Adhesion, Friction, and Surface Interactions
Keywords
mussel adhesive proteins, DOPA, single-molecule mechanics, non-covalent binding, bond dissociation energy, metal oxide surfaces, organic surfaces, covalent bonding, post-translational modification, hydrogen bonding, wet adhesion
MeSH terms
Adhesiveness, Amino Acid Sequence, Animals, Biomechanical Phenomena, Dihydroxyphenylalanine, Molecular Sequence Data, Oxidation-Reduction, Proteins, Titanium, Microscopy, Atomic Force, Bivalvia

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