Development of a caffeic acid-phthalimide hybrid compound for NADPH oxidase inhibition

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MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversidade Estadual Paulista (Unesp)-
Autor(es): dc.contributorUniversidade Estadual de Maringá (UEM)-
Autor(es): dc.creatorSantos, Willian Henrique dos [UNESP]-
Autor(es): dc.creatorYoguim, Maurício Ikeda [UNESP]-
Autor(es): dc.creatorDaré, Regina Gomes-
Autor(es): dc.creatorDa Silva-Filho, Luiz Carlos [UNESP]-
Autor(es): dc.creatorLautenschlager, Sueli Oliveira Silva-
Autor(es): dc.creatorXimenes, Valdecir Farias [UNESP]-
Data de aceite: dc.date.accessioned2022-02-22T00:54:12Z-
Data de disponibilização: dc.date.available2022-02-22T00:54:12Z-
Data de envio: dc.date.issued2021-06-25-
Data de envio: dc.date.issued2021-06-25-
Data de envio: dc.date.issued2021-05-12-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1039/d1ra01066b-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/208707-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/208707-
Descrição: dc.descriptionNADPH oxidases are pharmacological targets for the treatment of inflammation-based diseases. This work presents the synthesis and study of a caffeic acid/phthalimide hybrid compound (C2) as a potential inhibitor of NADPH oxidases. Throughout the study, we have compared compound C2 with its precursor caffeic acid (C1). The redox properties were compared using three different antioxidant methodologies and showed that C2 was slightly less effective than C1, a well-established and robust antioxidant. However, C2 was three-fold more effective than albumin (used as a model protein). This chemical feature was decisive for the higher efficiency of C2 as an inhibitor of the release of superoxide anions by stimulated neutrophils and enzymatic activity of cell-free NADPH oxidase. Docking simulation studies were performed using the crystal structure of the recombinant dehydrogenase domain of the isoform NOX5 of C. stagnale, which retains the FAD cofactor (PDB: 5O0X). Considering that C2 could bind at the FAD redox site of NOX5, studies were conducted by comparing the interactions and binding energies of C1 and C2. The binding energies were -50.30 (C1) and -74.88 (C2) (kJ mol-1), which is in agreement with the higher efficacy of the latter as an NADPH oxidase inhibitor. In conclusion, incorporating the phthalimide moiety into caffeic acid was decisive for its effectiveness as an NADPH oxidase inhibitor.-
Descrição: dc.descriptionDepartment of Chemistry Faculty of Sciences UNESP-São Paulo State University-
Descrição: dc.descriptionDepartment of Pharmaceutical Sciences Maringa State University (UEM)-
Descrição: dc.descriptionDepartment of Chemistry Faculty of Sciences UNESP-São Paulo State University-
Formato: dc.format17880-17890-
Idioma: dc.languageen-
Relação: dc.relationRSC Advances-
???dc.source???: dc.sourceScopus-
Título: dc.titleDevelopment of a caffeic acid-phthalimide hybrid compound for NADPH oxidase inhibition-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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