Use este identificador para citar ou linkar para este item: http://hdl.handle.net/1843/45404
Tipo: Artigo de Periódico
Título: Structural and dynamic insights of the interaction between tritrpticin and micelles: an NMR study
Autor(es): Talita Lopes dos Santos
Adolfo Henrique de Moraes Silva
Clovis Ryuichi Nakaie
Fabio C. L. Almeida
Shirley Schreier
Ana Paula Canedo Valente
Resumo: A 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.
Assunto: Peptídios
Micelas
Produtos de ação antimicrobiana
Espectroscopia de ressonância nuclear
Ressonância magnética nuclear
Idioma: eng
País: Brasil
Editor: Universidade Federal de Minas Gerais
Sigla da Instituição: UFMG
Departamento: ICX - DEPARTAMENTO DE QUÍMICA
Tipo de Acesso: Acesso Aberto
Identificador DOI: http://dx.doi.org/10.1016/j.bpj.2016.10.034
URI: http://hdl.handle.net/1843/45404
Data do documento: 27-Out-2016
metadata.dc.url.externa: https://www.sciencedirect.com/science/article/pii/S0006349516309936?via%3Dihub
metadata.dc.relation.ispartof: Biophysical journal (online)
Aparece nas coleções:Artigo de Periódico

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