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Cited by 167

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Molecular design principles of Lysine-DOPA wet adhesion

Open access
Li, Yiran, Cheng, Jing, Delparastan, Peyman, Wang, Haoqi, Sigg, Severin J., DeFrates, Kelsey G., Cao, Yi, Messersmith, Phillip B.·2020·Nature Communications

Abstract

The mussel byssus has long been a source of inspiration for the adhesion community. Recently, adhesive synergy between flanking lysine (Lys, K) and 3,4-Dihydroxyphenylalanine (DOPA, Y) residues in the mussel foot proteins (Mfps) has been highlighted. However, the complex topological relationship of DOPA and Lys as well as the interfacial adhesive roles of other amino acids have been understudied. Herein, we study adhesion of Lys and DOPA-containing peptides to organic and inorganic substrates using single-molecule force spectroscopy (SMFS). We show that a modest increase in peptide length, from K Y to (K Y)3, increases adhesion strength to TiO 2. Surprisingly, further increase in peptide length offers no additional benefit. Additionally, comparison of adhesion of dipeptides containing Lys and either DOPA (K Y) or phenylalanine (KF) shows that DOPA is stronger and more versatile. We furthermore demonstrate that incorporating a nonadhesive spacer between (K Y) repeats can mimic the hidden length in the Mfp and act as an effective strategy to dissipate energy.

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Metadata

Authors
Li, Y., Cheng, J., Delparastan, P., Wang, H., Sigg, S. J., DeFrates, K. G., Cao, Y., & Messersmith, P. B.
Venue
Nature Communications
Published
2020-08-04
Volume
11
Issue
1
Pages
3895-3895
ISSN
2041-1723 (ISSN-L)
OpenAlex
W3047371915
Cited by
167
References
2
FWCI
5.44
Type
journal article
Language
en
Open access
gold

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CoChat. (2026). Citation check: Molecular design principles of Lysine-DOPA wet adhesion. https://app.cochat.ai/papers/10.1038/s41467-020-17597-4
The paper
Li, Y., Cheng, J., Delparastan, P., Wang, H., Sigg, S. J., DeFrates, K. G., Cao, Y., & Messersmith, P. B. (2020). Molecular design principles of Lysine-DOPA wet adhesion. Nature Communications. https://doi.org/10.1038/s41467-020-17597-4

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