Biophysical studies of the interaction of hRSV Non-Structural 1 protein with natural flavonoids and their acetylated derivatives by spectroscopic techniques and computational simulations

Registro completo de metadados
MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.contributorFederal University of Rio de Janeiro-
Autor(es): dc.creatorOttenio de Lourenço, Isabella-
Autor(es): dc.creatorToscano Pedroso Quintino, Evelyn-
Autor(es): dc.creatorHenrique Pereira, Matheus-
Autor(es): dc.creatorSprengel Lima, Caroline-
Autor(es): dc.creatorCampos Araújo, Gabriela-
Autor(es): dc.creatorOctávio Regasini, Luis-
Autor(es): dc.creatorAlves de Melo, Fernando-
Autor(es): dc.creatorPereira de Souza, Fátima-
Autor(es): dc.creatorAndres Fossey, Marcelo-
Autor(es): dc.creatorPutinhon Caruso, Ícaro-
Data de aceite: dc.date.accessioned2025-08-21T15:51:35Z-
Data de disponibilização: dc.date.available2025-08-21T15:51:35Z-
Data de envio: dc.date.issued2023-03-01-
Data de envio: dc.date.issued2023-03-01-
Data de envio: dc.date.issued2022-12-14-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1016/j.saa.2022.121751-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/241506-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/241506-
Descrição: dc.descriptionHuman respiratory syncytial virus (hRSV) infections are one of the most causes of acute lower respiratory tract infections in children and elderly. The development of effective antiviral therapies or preventive vaccines against hRSV is not available yet. Thus, it is necessary to search for protein targets to combat this viral infection, as well as potential ways to block them. Non-Structural 1 (NS1) protein is an important factor for viral replication success since reduces the immune response by interacting with proteins in the type I interferon pathway. The influence of NS1 on the cell's immune response denotes the potential of its inhibition, being a possible target of treatment against hRSV infection. Here, it was studied the interaction of hRSV NS1 with natural flavonoids chrysin, morin, kaempferol, and myricetin and their mono-acetylated chrysin and penta-acetylated morin derivatives using spectroscopic techniques and computational simulations. The fluorescence data indicate that the binding affinities are on the order of 105 M−1, which are directly related to the partition coefficient of each flavonoid with Pearson's correlation coefficients of 0.76–0.80. The thermodynamic analysis suggests that hydrophobic interactions play a key role in the formation of the NS1/flavonoid complexes, with positive values of enthalpy and entropy changes. The computational approach proposes that flavonoids bind in a region of NS1 formed between the C-terminal α3-helix and the protein core, important for its biological function, and corroborate with experimental data revealing that hydrophobic contacts are important for the binding. Therefore, the present study provides relevant molecular details for the development of a possible new strategy to fight infections caused by hRSV.-
Descrição: dc.descriptionDepartment of Physics Institute of Biosciences Letters and Exact Sciences (IBILCE) São Paulo State University “Júlio de Mesquita Filho” (UNESP), SP-
Descrição: dc.descriptionMultiuser Center for Biomolecular Innovation (CMIB) Department of Physics Institute of Biosciences Letters and Exact Sciences (IBILCE) São Paulo State University “Júlio de Mesquita Filho” (UNESP), SP-
Descrição: dc.descriptionDepartment of Chemistry and Environmental Sciences Institute of Biosciences Letters and Exact Sciences (IBILCE) São Paulo State University “Júlio de Mesquita Filho” (UNESP), SP-
Descrição: dc.descriptionInstitute of Medical Biochemistry Leopoldo de Meis and National Center for Structural Biology and Bioimaging Federal University of Rio de Janeiro, RJ-
Descrição: dc.descriptionDepartment of Physics Institute of Biosciences Letters and Exact Sciences (IBILCE) São Paulo State University “Júlio de Mesquita Filho” (UNESP), SP-
Descrição: dc.descriptionMultiuser Center for Biomolecular Innovation (CMIB) Department of Physics Institute of Biosciences Letters and Exact Sciences (IBILCE) São Paulo State University “Júlio de Mesquita Filho” (UNESP), SP-
Descrição: dc.descriptionDepartment of Chemistry and Environmental Sciences Institute of Biosciences Letters and Exact Sciences (IBILCE) São Paulo State University “Júlio de Mesquita Filho” (UNESP), SP-
Idioma: dc.languageen-
Relação: dc.relationSpectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectComputational simulations-
Palavras-chave: dc.subjectFlavonoid-
Palavras-chave: dc.subjecthRSV-
Palavras-chave: dc.subjectNS1 protein-
Palavras-chave: dc.subjectSpectroscopic techniques-
Título: dc.titleBiophysical studies of the interaction of hRSV Non-Structural 1 protein with natural flavonoids and their acetylated derivatives by spectroscopic techniques and computational simulations-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

Não existem arquivos associados a este item.