Quercetin pentaacetate inhibits in vitro human respiratory syncytial virus adhesion
Autor(a) principal: | |
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Data de Publicação: | 2020 |
Outros Autores: | , , , , , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1016/j.virusres.2019.197805 http://hdl.handle.net/11449/198201 |
Resumo: | Human respiratory syncytial virus (hRSV) is one of the main etiological agents of diseases of the lower respiratory tract and is often responsible for the hospitalization of children and the elderly. To date, treatments are only palliative and there is no vaccine available. Natural products show exceptional structural diversity and they have played a vital role in drug research. Several investigations focused on applied structural modification of natural products to improved metabolic stability, solubility and biological actions them. Quercetin is a flavonoid that presents several biological activities, including anti-hRSV role. Some works criticize the pharmacological use of Quercetin because it has low solubility and low specificity. In this sense, we acetylated Quercetin structure and we used in vitro and in silico assays to compare anti-hRSV function between Quercetin (Q0) and its derivative molecule (Q1). Q1 shows lower cytotoxic effect than Q0 on HEp-2 cells. In addition, Q1 was more efficient than Q0 to protect HEp-2 cells infected with different multiplicity of infection (0.1–1 MOI). The virucidal effects of Q0 and Q1 suggest interaction between these molecules and viral particle. Dynamic molecular results suggest that Q0 and Q1 may interact with F-protein on hRSV surface in an important region to adhesion and viral infection. Q1 interaction with F-protein showed ΔG= -14.22 kcal/mol and it was more stable than Q0. Additional, MTT and plate assays confirmed that virucidal Q1 effects occurs during adhesion step of cycle hRSV replication. In conclusion, acetylation improves anti-hRSV Quercetin effects because Quercetin pentaacetate could interact with F-protein with lower binding energy and better stability to block viral adhesion. These results show alternative anti-hRSV strategy and contribute to drug discovery and development. |
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Quercetin pentaacetate inhibits in vitro human respiratory syncytial virus adhesionAntiviralFlavonoidsHEp-2 cellsIn silicoIn vitroRespiratory virusHuman respiratory syncytial virus (hRSV) is one of the main etiological agents of diseases of the lower respiratory tract and is often responsible for the hospitalization of children and the elderly. To date, treatments are only palliative and there is no vaccine available. Natural products show exceptional structural diversity and they have played a vital role in drug research. Several investigations focused on applied structural modification of natural products to improved metabolic stability, solubility and biological actions them. Quercetin is a flavonoid that presents several biological activities, including anti-hRSV role. Some works criticize the pharmacological use of Quercetin because it has low solubility and low specificity. In this sense, we acetylated Quercetin structure and we used in vitro and in silico assays to compare anti-hRSV function between Quercetin (Q0) and its derivative molecule (Q1). Q1 shows lower cytotoxic effect than Q0 on HEp-2 cells. In addition, Q1 was more efficient than Q0 to protect HEp-2 cells infected with different multiplicity of infection (0.1–1 MOI). The virucidal effects of Q0 and Q1 suggest interaction between these molecules and viral particle. Dynamic molecular results suggest that Q0 and Q1 may interact with F-protein on hRSV surface in an important region to adhesion and viral infection. Q1 interaction with F-protein showed ΔG= -14.22 kcal/mol and it was more stable than Q0. Additional, MTT and plate assays confirmed that virucidal Q1 effects occurs during adhesion step of cycle hRSV replication. In conclusion, acetylation improves anti-hRSV Quercetin effects because Quercetin pentaacetate could interact with F-protein with lower binding energy and better stability to block viral adhesion. These results show alternative anti-hRSV strategy and contribute to drug discovery and development.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Universidade Estadual Paulista UNESP (FCLAssis)Universidade Estadual Paulista UNESP IBILCECentro Multiusuário de Inovação Biomolecular (CMIB) Universidade Estadual Paulista UNESP IBILCEDepartment of Biology University of Rome Tor Vergata, Via della Ricerca Scientifica 1Universidade Estadual Paulista UNESP (FCLAssis)Universidade Estadual Paulista UNESP IBILCECentro Multiusuário de Inovação Biomolecular (CMIB) Universidade Estadual Paulista UNESP IBILCEFAPESP: 2014/12298-7Universidade Estadual Paulista (Unesp)University of Rome Tor VergataLopes, Bruno Rafael Pereira [UNESP]da Costa, Mirian Feliciano [UNESP]de Genova Ribeiro, Amanda [UNESP]Lima, Caroline Sprendel [UNESP]Caruso, Icaro Putinhon [UNESP]de Araújo, Gabriela Campos [UNESP]Kubo, Letícia Hiromi [UNESP]Iacovelli, FedericoFalconi, MattiaDesideri, Alessandrode Oliveira, Juliana [UNESP]Regasini, Luis Octávio [UNESP]Souza, Fátima Pereira [UNESP]Toledo, Karina Alves [UNESP]da Silva, Tiago Francisco [UNESP]2020-12-12T01:06:20Z2020-12-12T01:06:20Z2020-01-15info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1016/j.virusres.2019.197805Virus Research, v. 276.1872-74920168-1702http://hdl.handle.net/11449/19820110.1016/j.virusres.2019.1978052-s2.0-85075628715Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengVirus Researchinfo:eu-repo/semantics/openAccess2021-10-23T09:55:30Zoai:repositorio.unesp.br:11449/198201Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T13:39:26.479741Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Quercetin pentaacetate inhibits in vitro human respiratory syncytial virus adhesion |
title |
Quercetin pentaacetate inhibits in vitro human respiratory syncytial virus adhesion |
spellingShingle |
Quercetin pentaacetate inhibits in vitro human respiratory syncytial virus adhesion Lopes, Bruno Rafael Pereira [UNESP] Antiviral Flavonoids HEp-2 cells In silico In vitro Respiratory virus |
title_short |
Quercetin pentaacetate inhibits in vitro human respiratory syncytial virus adhesion |
title_full |
Quercetin pentaacetate inhibits in vitro human respiratory syncytial virus adhesion |
title_fullStr |
Quercetin pentaacetate inhibits in vitro human respiratory syncytial virus adhesion |
title_full_unstemmed |
Quercetin pentaacetate inhibits in vitro human respiratory syncytial virus adhesion |
title_sort |
Quercetin pentaacetate inhibits in vitro human respiratory syncytial virus adhesion |
author |
Lopes, Bruno Rafael Pereira [UNESP] |
author_facet |
Lopes, Bruno Rafael Pereira [UNESP] da Costa, Mirian Feliciano [UNESP] de Genova Ribeiro, Amanda [UNESP] Lima, Caroline Sprendel [UNESP] Caruso, Icaro Putinhon [UNESP] de Araújo, Gabriela Campos [UNESP] Kubo, Letícia Hiromi [UNESP] Iacovelli, Federico Falconi, Mattia Desideri, Alessandro de Oliveira, Juliana [UNESP] Regasini, Luis Octávio [UNESP] Souza, Fátima Pereira [UNESP] Toledo, Karina Alves [UNESP] da Silva, Tiago Francisco [UNESP] |
author_role |
author |
author2 |
da Costa, Mirian Feliciano [UNESP] de Genova Ribeiro, Amanda [UNESP] Lima, Caroline Sprendel [UNESP] Caruso, Icaro Putinhon [UNESP] de Araújo, Gabriela Campos [UNESP] Kubo, Letícia Hiromi [UNESP] Iacovelli, Federico Falconi, Mattia Desideri, Alessandro de Oliveira, Juliana [UNESP] Regasini, Luis Octávio [UNESP] Souza, Fátima Pereira [UNESP] Toledo, Karina Alves [UNESP] da Silva, Tiago Francisco [UNESP] |
author2_role |
author author author author author author author author author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) University of Rome Tor Vergata |
dc.contributor.author.fl_str_mv |
Lopes, Bruno Rafael Pereira [UNESP] da Costa, Mirian Feliciano [UNESP] de Genova Ribeiro, Amanda [UNESP] Lima, Caroline Sprendel [UNESP] Caruso, Icaro Putinhon [UNESP] de Araújo, Gabriela Campos [UNESP] Kubo, Letícia Hiromi [UNESP] Iacovelli, Federico Falconi, Mattia Desideri, Alessandro de Oliveira, Juliana [UNESP] Regasini, Luis Octávio [UNESP] Souza, Fátima Pereira [UNESP] Toledo, Karina Alves [UNESP] da Silva, Tiago Francisco [UNESP] |
dc.subject.por.fl_str_mv |
Antiviral Flavonoids HEp-2 cells In silico In vitro Respiratory virus |
topic |
Antiviral Flavonoids HEp-2 cells In silico In vitro Respiratory virus |
description |
Human respiratory syncytial virus (hRSV) is one of the main etiological agents of diseases of the lower respiratory tract and is often responsible for the hospitalization of children and the elderly. To date, treatments are only palliative and there is no vaccine available. Natural products show exceptional structural diversity and they have played a vital role in drug research. Several investigations focused on applied structural modification of natural products to improved metabolic stability, solubility and biological actions them. Quercetin is a flavonoid that presents several biological activities, including anti-hRSV role. Some works criticize the pharmacological use of Quercetin because it has low solubility and low specificity. In this sense, we acetylated Quercetin structure and we used in vitro and in silico assays to compare anti-hRSV function between Quercetin (Q0) and its derivative molecule (Q1). Q1 shows lower cytotoxic effect than Q0 on HEp-2 cells. In addition, Q1 was more efficient than Q0 to protect HEp-2 cells infected with different multiplicity of infection (0.1–1 MOI). The virucidal effects of Q0 and Q1 suggest interaction between these molecules and viral particle. Dynamic molecular results suggest that Q0 and Q1 may interact with F-protein on hRSV surface in an important region to adhesion and viral infection. Q1 interaction with F-protein showed ΔG= -14.22 kcal/mol and it was more stable than Q0. Additional, MTT and plate assays confirmed that virucidal Q1 effects occurs during adhesion step of cycle hRSV replication. In conclusion, acetylation improves anti-hRSV Quercetin effects because Quercetin pentaacetate could interact with F-protein with lower binding energy and better stability to block viral adhesion. These results show alternative anti-hRSV strategy and contribute to drug discovery and development. |
publishDate |
2020 |
dc.date.none.fl_str_mv |
2020-12-12T01:06:20Z 2020-12-12T01:06:20Z 2020-01-15 |
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.virusres.2019.197805 Virus Research, v. 276. 1872-7492 0168-1702 http://hdl.handle.net/11449/198201 10.1016/j.virusres.2019.197805 2-s2.0-85075628715 |
url |
http://dx.doi.org/10.1016/j.virusres.2019.197805 http://hdl.handle.net/11449/198201 |
identifier_str_mv |
Virus Research, v. 276. 1872-7492 0168-1702 10.1016/j.virusres.2019.197805 2-s2.0-85075628715 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Virus Research |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
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_ |
1808128258929065984 |