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Cited 6 time in webofscience Cited 7 time in scopus
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dc.contributor.authorShin, Mincheol-
dc.contributor.authorShin, Ji Yeon-
dc.contributor.authorKim, Kyeounghak-
dc.contributor.authorYang, Byeongseon-
dc.contributor.authorHan, Jeong Woo-
dc.contributor.authorKim, Nak-Kyoon-
dc.contributor.authorCha, Hyung Joon-
dc.date.available2020-03-13T00:50:04Z-
dc.date.created2020-03-04-
dc.date.issued2020-03-
dc.identifier.issn0021-9797-
dc.identifier.urihttp://oasis.postech.ac.kr/handle/2014.oak/101381-
dc.description.abstractIntensive 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.-
dc.languageEnglish-
dc.publisherACADEMIC PRESS INC ELSEVIER SCIENCE-
dc.subjectAdhesives-
dc.subjectAmino acids-
dc.subjectDensity functional theory-
dc.subjectMolecules-
dc.subjectMolluscs-
dc.subjectProteins-
dc.subject3 ,4-Dihydroxyphenylalanine-
dc.subjectAdhesive proteins-
dc.subjectDopa-
dc.subjectFlanking lysine-
dc.subjectMechanistic analysis-
dc.subjectMussel adhesion-
dc.subjectMussel adhesive proteins-
dc.subjectSynergetic effect-
dc.subjectAdhesion-
dc.subjectcatechol-
dc.subjectDOPA-
dc.subjectferric ion-
dc.subjectlysine-
dc.subjectmussel adhesive protein-
dc.subjectpeptide-
dc.subjectadhesion-
dc.subjectArticle-
dc.subjectcontrolled study-
dc.subjectdensity functional theory-
dc.subjectmolecule-
dc.subjectmussel-
dc.subjectnonhuman-
dc.subjectnuclear magnetic resonance-
dc.subjectpriority journal-
dc.subjectsurface property-
dc.subjectunderwater adhesion-
dc.titleThe position of lysine controls the catechol-mediated surface adhesion and cohesion in underwater mussel adhesion-
dc.typeArticle-
dc.type.rimsART-
dc.identifier.bibliographicCitationJOURNAL OF COLLOID AND INTERFACE SCIENCE, v.563, pp.168 - 176-
dc.identifier.wosid000510313700019-
dc.citation.endPage176-
dc.citation.startPage168-
dc.citation.titleJOURNAL OF COLLOID AND INTERFACE SCIENCE-
dc.citation.volume563-
dc.contributor.affiliatedAuthorShin, Mincheol-
dc.contributor.affiliatedAuthorKim, Kyeounghak-
dc.contributor.affiliatedAuthorHan, Jeong Woo-
dc.contributor.affiliatedAuthorCha, Hyung Joon-
dc.identifier.scopusid2-s2.0-85076711809-
dc.description.journalClass1-
dc.description.isOpenAccessN-
dc.type.docTypeArticle-
dc.subject.keywordPlusSINGLE-MOLECULE-
dc.subject.keywordPlusWET ADHESION-
dc.subject.keywordPlusPROTEIN-
dc.subject.keywordPlusDOPA-
dc.subject.keywordPlusREDOX-
dc.subject.keywordPlusPEPTIDES-
dc.subject.keywordPlusDYNAMICS-
dc.subject.keywordPlusKINETICS-
dc.subject.keywordPlusSYNERGY-
dc.subject.keywordPlusCATIONS-
dc.subject.keywordAuthorUnderwater adhesion-
dc.subject.keywordAuthorMussel adhesion-
dc.subject.keywordAuthorDopa-
dc.subject.keywordAuthorMussel adhesive proteins-
dc.subject.keywordAuthorFlanking lysine-

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한정우HAN, JEONG WOO
Dept. of Chemical Enginrg
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