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Surface-facilitated formation of polydopamine and its implications in melanogenesis

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dc.contributor.authorKim, Chan Yeon-
dc.contributor.authorKim, Yoonyoung-
dc.contributor.authorLee, Min Young-
dc.contributor.authorJo, Seong Ah-
dc.contributor.authorKim, Seung-Woo-
dc.contributor.authorKang, Sung Min-
dc.contributor.authorKim, Young-Kwan-
dc.contributor.authorKang, Kyungtae-
dc.date.accessioned2024-08-08T09:31:54Z-
dc.date.available2024-08-08T09:31:54Z-
dc.date.issued2023-02-
dc.identifier.issn0927-7765-
dc.identifier.issn1873-4367-
dc.identifier.urihttps://scholarworks.dongguk.edu/handle/sw.dongguk/20955-
dc.description.abstractThis manuscript examines influences of differently functionalized surfaces on the formation of solution-dispersed polydopamine (pDA). Glass vials functionalized with different functional groups provided a set of conditions with which the relationship between the area of active surface and the rate of pDA formation could be sys-tematically studied. The results suggest that charged and polar surfaces accelerate pDA formation in solution, with the effect of-NH2 surfaces being exceptionally strong. In the vials, pDA formed as both forms of dispersions in solution and films at solid-liquid interface. Further analyses confirmed that both forms of pDA formed with-NH2 surfaces were chemically similar to conventional pDA synthesized without help of functional surfaces. Among short peptide-based amyloid fibers with defined surface functional groups, and those displaying lysines (-NH2) greatly accelerated the formation of pDA, consistent with the results of-NH2-functionalized vials. The results suggest that pDA formation may be facilitated by surface functional groups of solid-liquid interfaces, and have implications for the overlooked roles of amyloid fibers in biological melanogenesis.-
dc.format.extent7-
dc.language영어-
dc.language.isoENG-
dc.publisherELSEVIER-
dc.titleSurface-facilitated formation of polydopamine and its implications in melanogenesis-
dc.typeArticle-
dc.publisher.location네델란드-
dc.identifier.doi10.1016/j.colsurfb.2022.113068-
dc.identifier.scopusid2-s2.0-85143765439-
dc.identifier.wosid000899382400002-
dc.identifier.bibliographicCitationColloids and Surfaces B: Biointerfaces, v.222, pp 1 - 7-
dc.citation.titleColloids and Surfaces B: Biointerfaces-
dc.citation.volume222-
dc.citation.startPage1-
dc.citation.endPage7-
dc.type.docTypeArticle-
dc.description.isOpenAccessY-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaBiophysics-
dc.relation.journalResearchAreaChemistry-
dc.relation.journalResearchAreaMaterials Science-
dc.relation.journalWebOfScienceCategoryBiophysics-
dc.relation.journalWebOfScienceCategoryChemistry, Physical-
dc.relation.journalWebOfScienceCategoryMaterials Science, Biomaterials-
dc.subject.keywordPlusDOPAMINE-
dc.subject.keywordPlusCHEMISTRY-
dc.subject.keywordPlusPMEL17-
dc.subject.keywordPlusNANOPARTICLES-
dc.subject.keywordPlusMELANINS-
dc.subject.keywordPlusGROWTH-
dc.subject.keywordPlusAGENT-
dc.subject.keywordPlusCELLS-
dc.subject.keywordPlusFILMS-
dc.subject.keywordPlusION-
dc.subject.keywordAuthorSurface -driven polymerization-
dc.subject.keywordAuthorPolydopamine-
dc.subject.keywordAuthorPeptides-
dc.subject.keywordAuthorAmyloids-
dc.subject.keywordAuthorMelanogenesis-
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