Please use this identifier to cite or link to this item:
http://hdl.handle.net/1843/76839
Type: | Artigo de Periódico |
Title: | Gallic acid as a Sestrin (SESN2) activator and potential obesity therapeutic agent: a molecular docking study |
Other Titles: | Ácido gálico como ativador de Sestrina (SESN2) e potencial agente terapêutico para obesidade: um estudo de encaixe molecular |
Authors: | Jaciara Neves Sousa Lorena Dos Reis Pereira Queiroz Alfredo Maurício Batista de Paula André Luiz Sena Guimarães Caroline Honaiser Lescano Charles Martins Aguilar Ivan Pires de Oliveira Sérgio Henrique Sousa Santos |
Abstract: | Sestrins (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. |
Subject: | Ácido gálico Polímeros Proteinas |
language: | eng |
metadata.dc.publisher.country: | Brasil |
Publisher: | Universidade Federal de Minas Gerais |
Publisher Initials: | UFMG |
metadata.dc.publisher.department: | ICA - INSTITUTO DE CIÊNCIAS AGRÁRIAS |
Rights: | Acesso Restrito |
metadata.dc.identifier.doi: | https://doi.org/10.1016/j.gene.2023.147683 |
URI: | http://hdl.handle.net/1843/76839 |
Issue Date: | 2023 |
metadata.dc.url.externa: | https://www.sciencedirect.com/science/article/pii/S0378111923005243?via%3Dihub |
metadata.dc.relation.ispartof: | Gene |
Appears in Collections: | Artigo de Periódico |
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.