Structural and dynamic insights of the interaction between tritrpticin and micelles: an NMR study
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 st...
| Autores: | , , , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2016 |
| País: | Brasil |
| Institución: | Universidade Federal de Minas Gerais (UFMG) |
| Repositorio: | Repositório Institucional da UFMG |
| Idioma: | inglés |
| OAI Identifier: | oai:repositorio.ufmg.br:1843/45404 |
| Acceso en línea: | http://dx.doi.org/10.1016/j.bpj.2016.10.034 http://hdl.handle.net/1843/45404 https://orcid.org/0000-0002-3344-4084 https://orcid.org/0000-0001-7057-1990 https://orcid.org/0000-0001-6046-7006 https://orcid.org/0000-0003-1326-9933 https://orcid.org/0000-0001-7219-1123 |
| Access Level: | acceso abierto |
| Palabra clave: | Antimicrobial peptides (AMPs) Membrane lipid Cathelicidin AMP Micelles Peptides Tritrpticin (TRP3) One-dimensional NMR Two-dimensional NMR 1-lauroyl-2-hydroxy-sn-glycero-3-phosphocholine (LLPC, zwitterionic) 1-myristoyl-2-hydroxy-sn-glycero-3-phospho-1′-rac-glycerol (LMPG, anionic) Peptídios Micelas Produtos de ação antimicrobiana Espectroscopia de ressonância nuclear Ressonância magnética nuclear |
| Sumario: | 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. |
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