Dengue fusion peptides in interaction with model membranes – a fluorescence study
Título del documento: Dengue fusion peptides in interaction with model membranes – a fluorescence study
Revista: Ecletica quimica
Base de datos:
Número de sistema: 000552511
ISSN: 0100-4670
Autores: 4
1
2
1
3
Instituciones: 1São Paulo State University, Institute of Chemistry, Araraquara, Brazil.,
2University of São Paulo, Faculty of Philosophy, Sciences and Letters of Ribeirão Preto, Ribeirão Preto, Brazil.São Paulo State University, School of Technology and Applied Sciences, Presidente Prudente, Brazil.,
3University of São Paulo, Faculty of Philosophy, Sciences and Letters of Ribeirão Preto, Ribeirão Preto, Brazil.,
4University of São Paulo, Faculty of Philosophy, Sciences and Letters of Ribeirão Preto, Ribeirão Preto, Brazil.Universidade Federal do Tocantins, Araguaína Campus, Araguaína, Brazil.,
Año:
Volumen: 46
Paginación: 30-40
País: Brasil
Idioma: Inglés
Resumen en inglés 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.
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