Structural and dynamic insights of the interaction between tritrpticin and micelles: an NMR study

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dc.creatorTalita Lopes dos Santos
dc.creatorAdolfo Henrique de Moraes Silva
dc.creatorClovis Ryuichi Nakaie
dc.creatorFabio C. L. Almeida
dc.creatorShirley Schreier
dc.creatorAna Paula Canedo Valente
dc.date.accessioned2022-09-23T00:03:24Z
dc.date.accessioned2025-09-09T01:06:20Z
dc.date.available2022-09-23T00:03:24Z
dc.date.issued2016-10-27
dc.description.sponsorshipCNPq - Conselho Nacional de Desenvolvimento Científico e Tecnológico
dc.description.sponsorshipFAPERJ - Fundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiro
dc.format.mimetypepdf
dc.identifier.doihttp://dx.doi.org/10.1016/j.bpj.2016.10.034
dc.identifier.issn1542-0086 (online)
dc.identifier.urihttps://hdl.handle.net/1843/45404
dc.languageeng
dc.publisherUniversidade Federal de Minas Gerais
dc.relation.ispartofBiophysical journal (online)
dc.rightsAcesso Aberto
dc.subjectPeptídios
dc.subjectMicelas
dc.subjectProdutos de ação antimicrobiana
dc.subjectEspectroscopia de ressonância nuclear
dc.subjectRessonância magnética nuclear
dc.subject.otherAntimicrobial peptides (AMPs)
dc.subject.otherMembrane lipid
dc.subject.otherCathelicidin AMP
dc.subject.otherMicelles
dc.subject.otherPeptides
dc.subject.otherTritrpticin (TRP3)
dc.subject.otherOne-dimensional NMR
dc.subject.otherTwo-dimensional NMR
dc.subject.other1-lauroyl-2-hydroxy-sn-glycero-3-phosphocholine (LLPC, zwitterionic)
dc.subject.other1-myristoyl-2-hydroxy-sn-glycero-3-phospho-1′-rac-glycerol (LMPG, anionic)
dc.titleStructural and dynamic insights of the interaction between tritrpticin and micelles: an NMR study
dc.typeArtigo de periódico
local.citation.epage2688
local.citation.issue12
local.citation.spage2676
local.citation.volume111
local.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.
local.identifier.orcidhttps://orcid.org/0000-0002-3344-4084
local.identifier.orcidhttps://orcid.org/0000-0001-7057-1990
local.identifier.orcidhttps://orcid.org/0000-0001-6046-7006
local.identifier.orcidhttps://orcid.org/0000-0003-1326-9933
local.identifier.orcidhttps://orcid.org/0000-0001-7219-1123
local.publisher.countryBrasil
local.publisher.departmentICX - DEPARTAMENTO DE QUÍMICA
local.publisher.initialsUFMG
local.url.externahttps://www.sciencedirect.com/science/article/pii/S0006349516309936?via%3Dihub

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