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

Talita Lopes dos Santos; Adolfo Henrique de Moraes Silva; Clovis Ryuichi Nakaie; Fabio C. L. Almeida; Shirley Schreier; Ana Paula Canedo Valente

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...

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Autores:	Talita Lopes dos Santos, Adolfo Henrique de Moraes Silva, Clovis Ryuichi Nakaie, Fabio C. L. Almeida, Shirley Schreier, Ana Paula Canedo Valente
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

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spelling	Structural and dynamic insights of the interaction between tritrpticin and micelles: an NMR studyAntimicrobial peptides (AMPs)Membrane lipidCathelicidin AMPMicellesPeptidesTritrpticin (TRP3)One-dimensional NMRTwo-dimensional NMR1-lauroyl-2-hydroxy-sn-glycero-3-phosphocholine (LLPC, zwitterionic)1-myristoyl-2-hydroxy-sn-glycero-3-phospho-1′-rac-glycerol (LMPG, anionic)PeptídiosMicelasProdutos de ação antimicrobianaEspectroscopia de ressonância nuclearRessonância magnética nuclearA 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.CNPq - Conselho Nacional de Desenvolvimento Científico e TecnológicoFAPERJ - Fundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de JaneiroUniversidade Federal de Minas GeraisBrasilICX - DEPARTAMENTO DE QUÍMICAUFMG2022-09-23T00:03:24Z2022-09-23T00:03:24Z2016-10-27info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlepdfapplication/pdfhttp://dx.doi.org/10.1016/j.bpj.2016.10.0341542-0086 (online)http://hdl.handle.net/1843/45404https://orcid.org/0000-0002-3344-4084https://orcid.org/0000-0001-7057-1990https://orcid.org/0000-0001-6046-7006https://orcid.org/0000-0003-1326-9933https://orcid.org/0000-0001-7219-1123engBiophysical journal (online)info:eu-repo/semantics/openAccessreponame:Repositório Institucional da UFMGinstname:Universidade Federal de Minas Gerais (UFMG)instacron:UFMGTalita Lopes dos SantosAdolfo Henrique de Moraes SilvaClovis Ryuichi NakaieFabio C. L. AlmeidaShirley SchreierAna Paula Canedo Valente2022-09-23T00:03:24Zoai:repositorio.ufmg.br:1843/45404Repositório InstitucionalPUBhttps://repositorio.ufmg.br/oairepositorio@ufmg.bropendoar:2022-09-23T00:03:24Repositório Institucional da UFMG - Universidade Federal de Minas Gerais (UFMG)false
dc.title.none.fl_str_mv	Structural and dynamic insights of the interaction between tritrpticin and micelles: an NMR study
title	Structural and dynamic insights of the interaction between tritrpticin and micelles: an NMR study
spellingShingle	Structural and dynamic insights of the interaction between tritrpticin and micelles: an NMR study Talita Lopes dos Santos 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
title_short	Structural and dynamic insights of the interaction between tritrpticin and micelles: an NMR study
title_full	Structural and dynamic insights of the interaction between tritrpticin and micelles: an NMR study
title_fullStr	Structural and dynamic insights of the interaction between tritrpticin and micelles: an NMR study
title_full_unstemmed	Structural and dynamic insights of the interaction between tritrpticin and micelles: an NMR study
title_sort	Structural and dynamic insights of the interaction between tritrpticin and micelles: an NMR study
dc.creator.none.fl_str_mv	Talita Lopes dos Santos Adolfo Henrique de Moraes Silva Clovis Ryuichi Nakaie Fabio C. L. Almeida Shirley Schreier Ana Paula Canedo Valente
author	Talita Lopes dos Santos
author_facet	Talita Lopes dos Santos Adolfo Henrique de Moraes Silva Clovis Ryuichi Nakaie Fabio C. L. Almeida Shirley Schreier Ana Paula Canedo Valente
author_role	author
author2	Adolfo Henrique de Moraes Silva Clovis Ryuichi Nakaie Fabio C. L. Almeida Shirley Schreier Ana Paula Canedo Valente
author2_role	author author author author author
dc.subject.por.fl_str_mv	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
topic	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
description	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.
publishDate	2016
dc.date.none.fl_str_mv	2016-10-27 2022-09-23T00:03:24Z 2022-09-23T00:03:24Z
dc.type.status.fl_str_mv	info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv	info:eu-repo/semantics/article
format	article
status_str	publishedVersion
dc.identifier.uri.fl_str_mv	http://dx.doi.org/10.1016/j.bpj.2016.10.034 1542-0086 (online) 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
url	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
identifier_str_mv	1542-0086 (online)
dc.language.iso.fl_str_mv	eng
language	eng
dc.relation.none.fl_str_mv	Biophysical journal (online)
dc.rights.driver.fl_str_mv	info:eu-repo/semantics/openAccess
eu_rights_str_mv	openAccess
dc.format.none.fl_str_mv	pdf application/pdf
dc.publisher.none.fl_str_mv	Universidade Federal de Minas Gerais Brasil ICX - DEPARTAMENTO DE QUÍMICA UFMG
publisher.none.fl_str_mv	Universidade Federal de Minas Gerais Brasil ICX - DEPARTAMENTO DE QUÍMICA UFMG
dc.source.none.fl_str_mv	reponame:Repositório Institucional da UFMG instname:Universidade Federal de Minas Gerais (UFMG) instacron:UFMG
instname_str	Universidade Federal de Minas Gerais (UFMG)
instacron_str	UFMG
institution	UFMG
reponame_str	Repositório Institucional da UFMG
collection	Repositório Institucional da UFMG
repository.name.fl_str_mv	Repositório Institucional da UFMG - Universidade Federal de Minas Gerais (UFMG)
repository.mail.fl_str_mv	repositorio@ufmg.br
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score	15.301603

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

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