The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Mussel adhesion – essential footwork
Open accessAbstract
Robust adhesion to wet, salt-encrusted, corroded and slimy surfaces has been an essential adaptation in the life histories of sessile marine organisms for hundreds of millions of years, but it remains a major impasse for technology. Mussel adhesion has served as one of many model systems providing a fundamental understanding of what is required for attachment to wet surfaces. Most polymer engineers have focused on the use of 3,4-dihydroxyphenyl-l-alanine (Dopa), a peculiar but abundant catecholic amino acid in mussel adhesive proteins. The premise of this Review is that although Dopa does have the potential for diverse cohesive and adhesive interactions, these will be difficult to achieve in synthetic homologs without a deeper knowledge of mussel biology; that is, how, at different length and time scales, mussels regulate the reactivity of their adhesive proteins. To deposit adhesive proteins onto target surfaces, the mussel foot creates an insulated reaction chamber with extreme reaction conditions such as low pH, low ionic strength and high reducing poise. These conditions enable adhesive proteins to undergo controlled fluid–fluid phase separation, surface adsorption and spreading, microstructure formation and, finally, solidification.
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Holten-Andersen, N., Harrington, M. J., Birkedal, H., Lee, B. P., Messersmith, P. B., Lee, K. Y. C., & Waite, J. H. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1015862108 · Cited by 1,597
Self-citationAdaptive synergy between catechol and lysine promotes wet adhesion by surface salt displacement
Maier, G. P., Rapp, M. V., Waite, J. H., Israelachvili, J. N., & Butler, A. (2015) · Science · doi:10.1126/science.aab0556 · Cited by 722
Self-citationStrong reversible Fe 3+ -mediated bridging between dopa-containing protein films in water
Zeng, H., Hwang, D. S., Israelachvili, J. N., & Waite, J. H. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1007416107 · Cited by 517
Self-citationMussel protein adhesion depends on interprotein thiol-mediated redox modulation
Yu, J., Wei, W., Danner, E., Ashley, R. K., Israelachvili, J. N., & Waite, J. H. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.630 · Cited by 463
Self-citationSchmitt, L., Ludwig, M., Gaub, H. E., & Tampé, R. (2000) · Biophysical Journal · doi:10.1016/s0006-3495(00)76863-9 · Cited by 171
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Lu, Y., Sharma, B., Soon, W. L., Shi, X., Zhao, T., Lim, Y. T., Sobota, R. M., Hoon, S., Pilloni, G., Usadi, A., et al. (2022) · Advanced Science · doi:10.1002/advs.202201444 · Cited by 23
Oxidized Dopamine Acrylamide Primer to Achieve Durable Resin–Dentin Bonding
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Metadata
- Authors
- Waite, J. H.
- Venue
- Journal of Experimental Biology
- Publisher
- The Company of Biologists
- Published
- 2017-02-15
- Volume
- 220
- Issue
- 4
- Pages
- 517-530
- ISSN
- 0022-0949 (ISSN-L)
- 1477-9145
- OpenAlex
- W2587914684
- Cited by
- 675
- References
- 5
- FWCI
- 20.79
- Type
- journal article
- Language
- en
- Open access
- green
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.