Dengue fusion peptides in interaction with model membranes-A fluorescence study
Autor(a) principal: | |
---|---|
Data de Publicação: | 2021 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.26850/1678-4618eqj.v46.1SI.2021.p30-40 http://hdl.handle.net/11449/221744 |
Resumo: | Dengue fever is a widespread infectious disease caused by Dengue viruses and responsible for millions of cases per year. One of the key steps during the infection is the fusion between the cell membrane and the lipidic bilayer of the virus, done by the glycoprotein envelope. At the tip of the envelope there is a fusion peptide widely conserved among the four known virus serotypes. Here dengue fusion peptides were studied in buffer solution and interacting with model membranes using fluorescence techniques. Peptides have the tryptophan residue exposed to aqueous environment when in buffer, while is exposed to a hydrophobic environment when interacting with negatively charged vesicles, as shown by the blue shift of fluorescence emission and increase in the lifetime decay. Fluorescence anisotropy results confirm that the residue is in a more restrictive environment when interacting with vesicles. Finally, fluorescence correlation spectroscopy results support the importance of electrostatic interaction, showing that dengue peptide promotes a significant increase in diameter of negatively charged vesicles, compared to the absence of effect in the size of neutral vesicles. |
id |
UNSP_f218ffd070f35ad959d1647d447d03a6 |
---|---|
oai_identifier_str |
oai:repositorio.unesp.br:11449/221744 |
network_acronym_str |
UNSP |
network_name_str |
Repositório Institucional da UNESP |
repository_id_str |
2946 |
spelling |
Dengue fusion peptides in interaction with model membranes-A fluorescence studyDengue virus peptideFluorescence spectroscopyLipid peptide interactionVesicles diffusion coefficientDengue fever is a widespread infectious disease caused by Dengue viruses and responsible for millions of cases per year. One of the key steps during the infection is the fusion between the cell membrane and the lipidic bilayer of the virus, done by the glycoprotein envelope. At the tip of the envelope there is a fusion peptide widely conserved among the four known virus serotypes. Here dengue fusion peptides were studied in buffer solution and interacting with model membranes using fluorescence techniques. Peptides have the tryptophan residue exposed to aqueous environment when in buffer, while is exposed to a hydrophobic environment when interacting with negatively charged vesicles, as shown by the blue shift of fluorescence emission and increase in the lifetime decay. Fluorescence anisotropy results confirm that the residue is in a more restrictive environment when interacting with vesicles. Finally, fluorescence correlation spectroscopy results support the importance of electrostatic interaction, showing that dengue peptide promotes a significant increase in diameter of negatively charged vesicles, compared to the absence of effect in the size of neutral vesicles.Faculty of Philosophy,Sciences and Letters of Ribeiraõ Preto University of Saõ PauloUniversidade Federal Do Tocantins, Araguaína CampusInstitute of Chemistry Saõ Paulo State UniversitySchool of Technology and Applied Sciences Saõ Paulo State UniversityUniversity of Saõ PauloUniversidade Federal Do TocantinsSaõ Paulo State UniversityOlivier, Danilo Da SilvaCespedes, Graziely FerreiraPazin, Wallance MoreiraCilli, Eduardo MaffudIto, Amando Siuiti2022-04-28T19:40:13Z2022-04-28T19:40:13Z2021-04-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article30-40http://dx.doi.org/10.26850/1678-4618eqj.v46.1SI.2021.p30-40Ecletica Quimica, v. 46, p. 30-40.1678-46180100-4670http://hdl.handle.net/11449/22174410.26850/1678-4618eqj.v46.1SI.2021.p30-402-s2.0-85105804567Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengEcletica Quimicainfo:eu-repo/semantics/openAccess2022-04-28T19:40:13Zoai:repositorio.unesp.br:11449/221744Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T23:35:57.337397Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Dengue fusion peptides in interaction with model membranes-A fluorescence study |
title |
Dengue fusion peptides in interaction with model membranes-A fluorescence study |
spellingShingle |
Dengue fusion peptides in interaction with model membranes-A fluorescence study Olivier, Danilo Da Silva Dengue virus peptide Fluorescence spectroscopy Lipid peptide interaction Vesicles diffusion coefficient |
title_short |
Dengue fusion peptides in interaction with model membranes-A fluorescence study |
title_full |
Dengue fusion peptides in interaction with model membranes-A fluorescence study |
title_fullStr |
Dengue fusion peptides in interaction with model membranes-A fluorescence study |
title_full_unstemmed |
Dengue fusion peptides in interaction with model membranes-A fluorescence study |
title_sort |
Dengue fusion peptides in interaction with model membranes-A fluorescence study |
author |
Olivier, Danilo Da Silva |
author_facet |
Olivier, Danilo Da Silva Cespedes, Graziely Ferreira Pazin, Wallance Moreira Cilli, Eduardo Maffud Ito, Amando Siuiti |
author_role |
author |
author2 |
Cespedes, Graziely Ferreira Pazin, Wallance Moreira Cilli, Eduardo Maffud Ito, Amando Siuiti |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
University of Saõ Paulo Universidade Federal Do Tocantins Saõ Paulo State University |
dc.contributor.author.fl_str_mv |
Olivier, Danilo Da Silva Cespedes, Graziely Ferreira Pazin, Wallance Moreira Cilli, Eduardo Maffud Ito, Amando Siuiti |
dc.subject.por.fl_str_mv |
Dengue virus peptide Fluorescence spectroscopy Lipid peptide interaction Vesicles diffusion coefficient |
topic |
Dengue virus peptide Fluorescence spectroscopy Lipid peptide interaction Vesicles diffusion coefficient |
description |
Dengue fever is a widespread infectious disease caused by Dengue viruses and responsible for millions of cases per year. One of the key steps during the infection is the fusion between the cell membrane and the lipidic bilayer of the virus, done by the glycoprotein envelope. At the tip of the envelope there is a fusion peptide widely conserved among the four known virus serotypes. Here dengue fusion peptides were studied in buffer solution and interacting with model membranes using fluorescence techniques. Peptides have the tryptophan residue exposed to aqueous environment when in buffer, while is exposed to a hydrophobic environment when interacting with negatively charged vesicles, as shown by the blue shift of fluorescence emission and increase in the lifetime decay. Fluorescence anisotropy results confirm that the residue is in a more restrictive environment when interacting with vesicles. Finally, fluorescence correlation spectroscopy results support the importance of electrostatic interaction, showing that dengue peptide promotes a significant increase in diameter of negatively charged vesicles, compared to the absence of effect in the size of neutral vesicles. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-04-01 2022-04-28T19:40:13Z 2022-04-28T19:40:13Z |
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/10.26850/1678-4618eqj.v46.1SI.2021.p30-40 Ecletica Quimica, v. 46, p. 30-40. 1678-4618 0100-4670 http://hdl.handle.net/11449/221744 10.26850/1678-4618eqj.v46.1SI.2021.p30-40 2-s2.0-85105804567 |
url |
http://dx.doi.org/10.26850/1678-4618eqj.v46.1SI.2021.p30-40 http://hdl.handle.net/11449/221744 |
identifier_str_mv |
Ecletica Quimica, v. 46, p. 30-40. 1678-4618 0100-4670 10.26850/1678-4618eqj.v46.1SI.2021.p30-40 2-s2.0-85105804567 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Ecletica Quimica |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
30-40 |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1808129534757699584 |