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Please use this identifier to cite or link to this item: http://hdl.handle.net/1843/76839
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dc.creatorJaciara Neves Sousapt_BR
dc.creatorLorena Dos Reis Pereira Queirozpt_BR
dc.creatorAlfredo Maurício Batista de Paulapt_BR
dc.creatorAndré Luiz Sena Guimarãespt_BR
dc.creatorCaroline Honaiser Lescanopt_BR
dc.creatorCharles Martins Aguilarpt_BR
dc.creatorIvan Pires de Oliveirapt_BR
dc.creatorSérgio Henrique Sousa Santospt_BR
dc.date.accessioned2024-09-24T12:49:31Z-
dc.date.available2024-09-24T12:49:31Z-
dc.date.issued2023-
dc.citation.volume883pt_BR
dc.citation.spage1pt_BR
dc.citation.epage8pt_BR
dc.identifier.doihttps://doi.org/10.1016/j.gene.2023.147683pt_BR
dc.identifier.issn0378-1119pt_BR
dc.identifier.urihttp://hdl.handle.net/1843/76839-
dc.description.resumoSestrins (SESNs) are a family of evolutionarily conserved proteins among mammals. They have several body homeostatic functions such as antioxidant, metabolic, and anti-aging, and are required to regenerate hyperoxidized forms of peroxiredoxins and reactive oxygen species. Sestrin 2 has been studied as a therapeutic agent in obesity treatment. Gallic acid (GA) is a triphenolic compound with beneficial biological activities including anti-inflammatory, antidiabetic, antihypertensive, and antioxidant effects. Recent studies demonstrated the GA's ability to reduce body weight gain and improve glycemic parameters. In this sense, the present study aims to investigate the GA activating potential of Sestrin using the molecular docking method. The 3D structure of gallic acid was retrieved from the NCBI PubChem database and the chemical structure of the Sestrin2 protein from the RCSB Protein Data Bank (5DJ4). The docking calculus was performed via UCSF Chimera and AutoDock Vinaprograms. The results showed that amino acids Arg390, Glu451, Trp444, Thr386, Arg448, Thr374, Tyr375, Asn376, Thr377, Leu389, His454, Ser450, His86, and Val455 are very important for GA stabilization, resembling the interactions that permit Leucine to activate SESN2. In this context, the obesity therapeutic property of GA can be understood from a Sestrin activating process through amino acid metabolism.pt_BR
dc.description.sponsorshipCNPq - Conselho Nacional de Desenvolvimento Científico e Tecnológicopt_BR
dc.description.sponsorshipFAPEMIG - Fundação de Amparo à Pesquisa do Estado de Minas Geraispt_BR
dc.description.sponsorshipCAPES - Coordenação de Aperfeiçoamento de Pessoal de Nível Superiorpt_BR
dc.description.sponsorshipOutra Agênciapt_BR
dc.languageengpt_BR
dc.publisherUniversidade Federal de Minas Geraispt_BR
dc.publisher.countryBrasilpt_BR
dc.publisher.departmentICA - INSTITUTO DE CIÊNCIAS AGRÁRIASpt_BR
dc.publisher.initialsUFMGpt_BR
dc.relation.ispartofGene-
dc.rightsAcesso Restritopt_BR
dc.subjectÁcido gálicopt_BR
dc.subjectPolímerospt_BR
dc.subjectProteinaspt_BR
dc.subject.otherÁcido gálicopt_BR
dc.subject.otherPolímerospt_BR
dc.subject.otherProteinaspt_BR
dc.titleGallic acid as a Sestrin (SESN2) activator and potential obesity therapeutic agent: a molecular docking studypt_BR
dc.title.alternativeÁcido gálico como ativador de Sestrina (SESN2) e potencial agente terapêutico para obesidade: um estudo de encaixe molecularpt_BR
dc.typeArtigo de Periódicopt_BR
dc.url.externahttps://www.sciencedirect.com/science/article/pii/S0378111923005243?via%3Dihubpt_BR
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