Cited by 109Polymer Surface Interaction StudiesMarine Biology and Environmental ChemistryAdhesion, Friction, and Surface Interactions

Structure and sequence features of mussel adhesive protein lead to its salt-tolerant adhesion ability

Open access
Ou, Xinwen, Xue, Bin, Lao, Yichong, Wutthinitikornkit, Yanee, Tian, Ranran, Zou, Aodong, Yang, Lingyun, Wang, Wei +2 more·2020·Science Advances

Abstract

Aromatic and basic residue form pair in intrinsically disordered adhesive protein, and such pairs dominate protein adsorption.

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Crossref · 10.1126/sciadv.abb7620

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87 of 87 references verified0 citation errors · 0 not checkable

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  • BA and PEA effectively expel water from the contact interface, and when neighbouring with ATAC, they could enhance electrostatic interactions with the negatively charged glass surface.

    “This is because BA and PEA effectively expel water from the contact interface, and, when neighbouring with ATAC (Supplementary Fig. 11), they could enhance electrostatic interactions with the negatively charged glass surface27,40–43 (Supplementary Fig. 12).”

    From Data-driven de novo design of super-adhesive hydrogels (2025) · cites this paper as [42]

    The Discussion (page not provided) describes an analogous mechanism: aromatic Dopa or Tyr residues scatter interfacial water, allowing paired positively charged residues to bind electrostatically to negatively charged sites on mica. The paper does not establish that BA or PEA expel water or that pairing them with ATAC enhances interactions with glass. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

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Authors
Ou, X., Xue, B., Lao, Y., Wutthinitikornkit, Y., Tian, R., Zou, A., Yang, L., Wang, W., Cao, Y., & Li, J.
Affiliations
  • Zhejiang University (CN)
  • Collaborative Innovation Center of Advanced Microstructures (CN)
  • ShanghaiTech University (CN)
Corresponding author
  • Ou, Xinwen
  • Xue, Bin
  • Cao, Yi
  • Li, Jingyuan
Venue
Science Advances
Published
2020-09-25
Volume
6
Issue
39
ISSN
2375-2548 (ISSN-L)
OpenAlex
W3088203618
Cited by
109
References
87
Citations by year
2026: 25 · 2025: 28 · 2024: 14 · 2023: 17 · 2022: 8 · 2021: 16 · 2020: 1
FWCI
2.89
Type
journal article
Language
en
Open access
Locations
  • Science Advances (publishedVersion, cc-by-nc)
  • PubMed Central (publishedVersion, cc-by-nc)
  • PubMed (publishedVersion)
Funders
  • National Natural Science Foundation of China (11722434, 11874319, 11674153, 21904088, 11804148)
  • China Postdoctoral Science Foundation (2018M642401, 2019T120499)
  • National Natural Science Foundation of Jiangsu Province (BK2018032)
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, wet adhesion, DOPA, tyrosine, intrinsically disordered proteins, basic residues, protein conformation, surface binding, post-translational modification

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