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The position of lysine controls the catechol-mediated surface adhesion and cohesion in underwater mussel adhesion

Title
The position of lysine controls the catechol-mediated surface adhesion and cohesion in underwater mussel adhesion
Authors
Shin, MincheolShin, Ji YeonKim, KyeounghakYang, ByeongseonHan, Jeong WooKim, Nak-KyoonCha, Hyung Joon
Date Issued
Mar-2020
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Abstract
Intensive studies have found that 3,4-dihydroxyphenylalanine (Dopa) is one of the key molecules for underwater mussel adhesion. Although basic mechanisms of mussel adhesion have been elucidated, little is known about how mussels control the balance between surface adhesion and cohesion, which is critical for successful adhesion without peeling and/or tearing. In this work, we focused on lysine (Lys) molecules which are frequently flanked to Dopa residues in interfacial adhesive proteins, specifically their synergy and anti-synergy on surface adhesion and cohesion. Three model peptides were designed to characterize flanking Lys effects. Through nano-mechanistic analyses, we found that flanking Lys enhanced surface adhesion but disrupted Fe3+-mediated cohesion. Through nuclear magnetic resonance analyses and density functional theory calculations, we corroborated the synergetic effect on surface adhesion and anti-synergetic effect on cohesion. We also confirmed the consistency of flanking Lys effects in the actual protein system. Thus, we, for the first time, discovered that each Dopa molecule in interfacial adhesive proteins is participated in surface adhesion and cohesion differently through controlling the existence of flanking Lys. Our discovery enlightens how nature designs adhesive proteins through according roles of Dopa. (C) 2019 Elsevier Inc. All rights reserved.
URI
http://oasis.postech.ac.kr/handle/2014.oak/101381
ISSN
0021-9797
Article Type
Article
Citation
JOURNAL OF COLLOID AND INTERFACE SCIENCE, vol. 563, page. 168 - 176, 2020-03
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 HAN, JEONG WOO
Dept. of Chemical Enginrg
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