Cited by 723Polymer Surface Interaction StudiesMarine Biology and Environmental ChemistryAdhesion, Friction, and Surface Interactions

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Adaptive synergy between catechol and lysine promotes wet adhesion by surface salt displacement

Maier, Greg P., Rapp, Michael V., Waite, J. Herbert, Israelachvili, Jacob N., Butler, Alison·2015·Science

DOI 10.1126/science.aab0556

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Abstract

In physiological fluids and seawater, adhesion of synthetic polymers to solid surfaces is severely limited by high salt, pH, and hydration, yet these conditions have not deterred the evolution of effective adhesion by mussels. Mussel foot proteins provide insights about adhesive adaptations: Notably, the abundance and proximity of catecholic Dopa (3,4-dihydroxyphenylalanine) and lysine residues hint at a synergistic interplay in adhesion. Certain siderophores—bacterial iron chelators—consist of paired catechol and lysine functionalities, thereby providing a convenient experimental platform to explore molecular synergies in bioadhesion. These siderophores and synthetic analogs exhibit robust adhesion energies (E(ad) ≥-15 millijoules per square meter) to mica in saline pH 3.5 to 7.5 and resist oxidation. The adjacent catechol-lysine placement provides a "one-two punch," whereby lysine evicts hydrated cations from the mineral surface, allowing catechol binding to underlying oxides.

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Authors: Maier, G. P., Rapp, M. V., Waite, J. H., Israelachvili, J. N., & Butler, A.
Affiliations: University of California, Santa Barbara (US)
Corresponding author: Maier, Greg P.
Rapp, Michael V.
Waite, J. Herbert
Israelachvili, Jacob N.
Butler, Alison
ORCID: Waite, J. Herbert
Israelachvili, Jacob N.
Butler, Alison
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2015-08-07
Volume: 349
Issue: 6248
Pages: 628-632
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.aab0556
OpenAlex: W1585589485
Cited by: 722
References: 30
Citations by year: 2026: 44 · 2025: 63 · 2024: 64 · 2023: 80 · 2022: 96 · 2021: 98 · 2020: 66 · 2019: 58 · 2018: 61 · 2017: 55 · 2016: 33 · 2015: 4
FWCI: 19.82
Type: journal article
Language: en
Open access: closed
Licence: www.sciencemag.org/about/science-licenses-journal-article-reuse (vor, 366 d)
Locations: Science (publishedVersion)
PubMed (publishedVersion)
eScholarship (California Digital Library) (submittedVersion)
Funders: National Science Foundation (DMR 1121053)
NSF (CHE-1411942)
NSF GRFP
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: wet adhesion, catechol, lysine, mussel foot proteins, DOPA, siderophores, bioadhesion, synthetic polymers, mica, saline environment, adhesion energy, iron chelators
MeSH terms: Adhesiveness, Adhesives, Aluminum Silicates, Catechols, Dihydroxyphenylalanine, Hydrogen-Ion Concentration, Lysine, Oxidation-Reduction, Proteins, Titanium, Siderophores, Molecular Mimicry

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Adaptive synergy between catechol and lysine promotes wet adhesion by surface salt displacement

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