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

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dc.contributor.authorOttenio de Lourenço, Isabella [UNESP]
dc.contributor.authorToscano Pedroso Quintino, Evelyn [UNESP]
dc.contributor.authorHenrique Pereira, Matheus [UNESP]
dc.contributor.authorSprengel Lima, Caroline [UNESP]
dc.contributor.authorCampos Araújo, Gabriela [UNESP]
dc.contributor.authorOctávio Regasini, Luis [UNESP]
dc.contributor.authorAlves de Melo, Fernando [UNESP]
dc.contributor.authorPereira de Souza, Fátima [UNESP]
dc.contributor.authorAndres Fossey, Marcelo [UNESP]
dc.contributor.authorPutinhon Caruso, Ícaro [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)
dc.contributor.institutionFederal University of Rio de Janeiro
dc.date.accessioned2023-03-01T21:06:59Z
dc.date.available2023-03-01T21:06:59Z
dc.date.issued2022-12-15
dc.description.abstractHuman 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.en
dc.description.affiliationDepartment of Physics Institute of Biosciences Letters and Exact Sciences (IBILCE) São Paulo State University “Júlio de Mesquita Filho” (UNESP), SP
dc.description.affiliationMultiuser 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
dc.description.affiliationDepartment of Chemistry and Environmental Sciences Institute of Biosciences Letters and Exact Sciences (IBILCE) São Paulo State University “Júlio de Mesquita Filho” (UNESP), SP
dc.description.affiliationInstitute of Medical Biochemistry Leopoldo de Meis and National Center for Structural Biology and Bioimaging Federal University of Rio de Janeiro, RJ
dc.description.affiliationUnespDepartment of Physics Institute of Biosciences Letters and Exact Sciences (IBILCE) São Paulo State University “Júlio de Mesquita Filho” (UNESP), SP
dc.description.affiliationUnespMultiuser 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
dc.description.affiliationUnespDepartment of Chemistry and Environmental Sciences Institute of Biosciences Letters and Exact Sciences (IBILCE) São Paulo State University “Júlio de Mesquita Filho” (UNESP), SP
dc.identifierhttp://dx.doi.org/10.1016/j.saa.2022.121751
dc.identifier.citationSpectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy, v. 283.
dc.identifier.doi10.1016/j.saa.2022.121751
dc.identifier.issn1386-1425
dc.identifier.scopus2-s2.0-85135882461
dc.identifier.urihttp://hdl.handle.net/11449/241506
dc.language.isoeng
dc.relation.ispartofSpectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy
dc.sourceScopus
dc.subjectComputational simulations
dc.subjectFlavonoid
dc.subjecthRSV
dc.subjectNS1 protein
dc.subjectSpectroscopic techniques
dc.titleBiophysical studies of the interaction of hRSV Non-Structural 1 protein with natural flavonoids and their acetylated derivatives by spectroscopic techniques and computational simulationsen
dc.typeArtigo

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