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The position of lysine controls the catechol-mediated surface adhesion…

Year of publication
Title of paper
The position of lysine controls the catechol-mediated surface adhesion and cohesion in underwater mussel adhesion
Author
[차형준교수, 한정우교수 연구실]
Publication in journal
Journal of Colloid and Interface Science 563, p168-176, 2019
Publication date
20200315



[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.

 

DOI: 10.1016/j.jcis.2019.12.082

LINK: https://www.sciencedirect.com/science/article/pii/S0021979719315504?dgc