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Please use this identifier to cite or link to this item: http://hdl.handle.net/1843/45404
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dc.creatorTalita Lopes dos Santospt_BR
dc.creatorAdolfo Henrique de Moraes Silvapt_BR
dc.creatorClovis Ryuichi Nakaiept_BR
dc.creatorFabio C. L. Almeidapt_BR
dc.creatorShirley Schreierpt_BR
dc.creatorAna Paula Canedo Valentept_BR
dc.date.accessioned2022-09-23T00:03:24Z-
dc.date.available2022-09-23T00:03:24Z-
dc.date.issued2016-10-27-
dc.citation.volume111pt_BR
dc.citation.issue12pt_BR
dc.citation.spage2676pt_BR
dc.citation.epage2688pt_BR
dc.identifier.doihttp://dx.doi.org/10.1016/j.bpj.2016.10.034pt_BR
dc.identifier.issn1542-0086 (online)pt_BR
dc.identifier.urihttp://hdl.handle.net/1843/45404-
dc.description.resumoA large number of antimicrobial peptides (AMPs) acts with high selectivity and specificity through interactions with membrane lipid components. These peptides undergo complex conformational changes in solution; upon binding to an interface, one major conformation is stabilized. Here we describe a study of the interaction between tritrpticin (TRP3), a cathelicidin AMP, and micelles of different chemical composition. The peptide’s structure and dynamics were examined using one-dimensional and two-dimensional NMR. Our data showed that the interaction occurred by conformational selection and the peptide acquired similar structures in all systems studied, despite differences in detergent headgroup charge or dipole orientation. Fluorescence and paramagnetic relaxation enhancement experiments showed that the peptide is located in the interface region and is slightly more deeply inserted in 1-myristoyl-2-hydroxy-sn-glycero-3-phospho-1′-rac-glycerol (LMPG, anionic) than in 1-lauroyl-2-hydroxy-sn-glycero-3-phosphocholine (LLPC, zwitterionic) micelles. Moreover, the tilt angle of an assumed helical portion of the peptide is similar in both systems. In previous work we proposed that TRP3 acts by a toroidal pore mechanism. In view of the high hydrophobic core exposure, hydration, and curvature presented by micelles, the conformation of TRP3 in these systems could be related to the peptide’s conformation in the toroidal pore.pt_BR
dc.description.sponsorshipCNPq - Conselho Nacional de Desenvolvimento Científico e Tecnológicopt_BR
dc.description.sponsorshipFAPERJ - Fundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiropt_BR
dc.format.mimetypepdfpt_BR
dc.languageengpt_BR
dc.publisherUniversidade Federal de Minas Geraispt_BR
dc.publisher.countryBrasilpt_BR
dc.publisher.departmentICX - DEPARTAMENTO DE QUÍMICApt_BR
dc.publisher.initialsUFMGpt_BR
dc.relation.ispartofBiophysical journal (online)pt_BR
dc.rightsAcesso Abertopt_BR
dc.subjectAntimicrobial peptides (AMPs)pt_BR
dc.subjectMembrane lipidpt_BR
dc.subjectCathelicidin AMPpt_BR
dc.subjectMicellespt_BR
dc.subjectPeptidespt_BR
dc.subjectTritrpticin (TRP3)pt_BR
dc.subjectOne-dimensional NMRpt_BR
dc.subjectTwo-dimensional NMRpt_BR
dc.subject1-lauroyl-2-hydroxy-sn-glycero-3-phosphocholine (LLPC, zwitterionic)pt_BR
dc.subject1-myristoyl-2-hydroxy-sn-glycero-3-phospho-1′-rac-glycerol (LMPG, anionic)pt_BR
dc.subject.otherPeptídiospt_BR
dc.subject.otherMicelaspt_BR
dc.subject.otherProdutos de ação antimicrobianapt_BR
dc.subject.otherEspectroscopia de ressonância nuclearpt_BR
dc.subject.otherRessonância magnética nuclearpt_BR
dc.titleStructural and dynamic insights of the interaction between tritrpticin and micelles: an NMR studypt_BR
dc.typeArtigo de Periódicopt_BR
dc.url.externahttps://www.sciencedirect.com/science/article/pii/S0006349516309936?via%3Dihubpt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-3344-4084pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0001-7057-1990pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0001-6046-7006pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0003-1326-9933pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0001-7219-1123pt_BR
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