Gallic Acid as a Non-Selective Inhibitor of α/β-Hydrolase Fold Enzymes Involved in the Inflammatory Process: The Two Sides of the Same Coin

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Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.contributorFederal University of ABC-
Autor(es): dc.creatorToyama, Marcos Hikari-
Autor(es): dc.creatorRogero, Airam-
Autor(es): dc.creatorde Moraes, Laila Lucyane Ferreira-
Autor(es): dc.creatorFernandes, Gustavo Antônio-
Autor(es): dc.creatorCosta, Caroline Ramos da Cruz-
Autor(es): dc.creatorBelchor, Mariana Novo-
Autor(es): dc.creatorDe Carli, Agatha Manzi-
Autor(es): dc.creatorde Oliveira, Marcos Antônio-
Data de aceite: dc.date.accessioned2025-08-21T22:05:29Z-
Data de disponibilização: dc.date.available2025-08-21T22:05:29Z-
Data de envio: dc.date.issued2022-05-01-
Data de envio: dc.date.issued2022-05-01-
Data de envio: dc.date.issued2022-01-31-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.3390/pharmaceutics14020368-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/234122-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/234122-
Descrição: dc.description(1) Background: Gallic acid (GA) has been characterized as an effective anti-inflammatory, antivenom, and promising drug for therapeutic use. (2/3) Methods and Results: GA was identified from ethanolic extract of fresh pitanga (Eugenia uniflora) leaves, which was identified using commercial GA. Commercial GA neutralized the enzymatic activity of secretory PLA2 (sPLA2) by inhibiting the active site and inducing changes in the secondary structure of the enzyme. Pharmacological edema assays showed that GA strongly decreased edema when the compound was previously incubated with sPLA2. However, prior treatment of GA (30 min before) significantly increased the edema and myotoxicity induced by sPLA2. The molecular docking results of GA with platelet-acetylhydrolase (PAF-AH) and acetylcholinesterase reveal that this compound was able to interact with the active site of both molecules, inhibiting the hydrolysis of platelet-activating factor (PAF) and acetylcholine (ACh). (4) Conclusion: GA has a great potential application; however, our results show that this compound can also induce adverse effects in previously treated animals. Additionally, the increased edema and myotoxicity observed experimentally in GA-treated animals may be due to the inhibition of PAF-AH and Acetylcholinesterase.-
Descrição: dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
Descrição: dc.descriptionBIOMOLPEP Group Biosciences Institute São Paulo State University (UNESP), São Paulo-
Descrição: dc.descriptionPostgraduate Program in Biotechnosciences Federal University of ABC, São Paulo-
Descrição: dc.descriptionBIOMOLPEP Group Biosciences Institute São Paulo State University (UNESP), São Paulo-
Descrição: dc.descriptionCNPq: 2019 304153/2019-2-
Idioma: dc.languageen-
Relação: dc.relationPharmaceutics-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectEdema-
Palavras-chave: dc.subjectGallic acid-
Palavras-chave: dc.subjectMyotoxic effect-
Palavras-chave: dc.subjectPhospholipase A2-
Palavras-chave: dc.subjectSnake venom-
Título: dc.titleGallic Acid as a Non-Selective Inhibitor of α/β-Hydrolase Fold Enzymes Involved in the Inflammatory Process: The Two Sides of the Same Coin-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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