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Cited by 297

The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.

Adaptive hydrophobic and hydrophilic interactions of mussel foot proteins with organic thin films

Open access
Yu, Jing, Kan, Yajing, Rapp, Michael, Danner, Eric, Wei, Wei, Das, Saurabh, Miller, Dusty R., Chen, Yunfei, Waite, J. Herbert, Israelachvili, Jacob N.·2013·Proceedings of the National Academy of Sciences

Abstract

Significance: Two popular perceptions about the much-mimicked adhesion of mussels are ( i ) the adhesion depends entirely on 3, 4-dihydroxyphenylalanine (Dopa) groups (benzene derivatives with two H-bonding prongs) and ( ii ) Dopa can stick to all surfaces. This study shows that both perceptions are incorrect: using three Dopa-containing mussel foot proteins (Mfps) on two chemically different self-assembled monolayers (SAM), we found the highest adhesion on the nonpolar (i.e., hydrophobic) SAMs was exhibited by the Mfp with the most hydrophobic side chains, not the most Dopa. Furthermore, increasing the spacing between the H-bond acceptors in the SAMs prevented the double-pronged H-bonding of Dopa side chains to polar SAMs. These findings clarify the roles of hydrophobic and hydrophilic interactions in both biological and nonbiological adhesion.

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Metadata

Authors
Yu, J., Kan, Y., Rapp, M., Danner, E., Wei, W., Das, S., Miller, D. R., Chen, Y., Waite, J. H., & Israelachvili, J. N.
Venue
Proceedings of the National Academy of Sciences
Published
2013-09-06
Volume
110
Issue
39
Pages
15680-15685
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1968489453
Cited by
297
References
29
FWCI
5.13
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Adaptive hydrophobic and hydrophilic interactions of mussel foot proteins with organic thin films. https://app.cochat.ai/papers/10.1073/pnas.1315015110
The paper
Yu, J., Kan, Y., Rapp, M., Danner, E., Wei, W., Das, S., Miller, D. R., Chen, Y., Waite, J. H., & Israelachvili, J. N. (2013). Adaptive hydrophobic and hydrophilic interactions of mussel foot proteins with organic thin films. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1315015110

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