Molecular design principles of Lysine-DOPA wet adhesion

Yiran Li, Jing Cheng, Peyman Delparastan, Haoqi Wang, Severin J. Sigg, Kelsey G. DeFrates, Yi Cao and Phillip B. Messersmith ()
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Yiran Li: University of California
Jing Cheng: University of California
Peyman Delparastan: University of California
Haoqi Wang: Nanjing University
Severin J. Sigg: University of California
Kelsey G. DeFrates: University of California
Yi Cao: Nanjing University
Phillip B. Messersmith: University of California

Nature Communications, 2020, vol. 11, issue 1, 1-8

Abstract: 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 KY to (KY)3, increases adhesion strength to TiO2. Surprisingly, further increase in peptide length offers no additional benefit. Additionally, comparison of adhesion of dipeptides containing Lys and either DOPA (KY) or phenylalanine (KF) shows that DOPA is stronger and more versatile. We furthermore demonstrate that incorporating a nonadhesive spacer between (KY) repeats can mimic the hidden length in the Mfp and act as an effective strategy to dissipate energy.

Date: 2020
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DOI: 10.1038/s41467-020-17597-4

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