{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["10"],"submitter":["Zhu H"],"pubmed_abstract":["Six flavonoid derivatives were synthesized and tested for anti-α-glucosidase activities. All derivatives were confirmed using NMR and HRMS and exhibited excellent inhibitory effects on α-glucosidase. Derivative four exhibited the highest anti-α-glucosidase activity (IC50: 15.71 ± 0.21 μM). Structure-activity relationship results showed that bromine group would be the most beneficial group to anti-α-glucosidase activity. Inhibitory mechnism and inhibition kinetics results showed derivative four was a reversible and mixed-type inhibitor. Molecular docking revealed that derivative four was tightly bind to the amino acid residues of active pocket of α-glucosidase and formed hydrogen bond, π-π stacking, and Pi-Donor hydrogen with α-glucosidase. Moreover, the physicochemical parameters of all derivatives were assessed using SwissADME software. This results also showed that the hybridization of flavonoid and phenylpropionic acid would be a useful strategy for the development of α-glucosidase inhibitors."],"journal":["Frontiers in chemistry"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9705736"],"repository":["biostudies-literature"],"pubmed_title":["Synthesis of activity evaluation of flavonoid derivatives as ɑ-glucosidase inhibitors"],"pmcid":["PMC9705736"],"pubmed_authors":["Zhu H","Zhong X"],"additional_accession":[]},"is_claimable":false,"name":"Synthesis of activity evaluation of flavonoid derivatives as ɑ-glucosidase inhibitors","description":"Six flavonoid derivatives were synthesized and tested for anti-α-glucosidase activities. All derivatives were confirmed using NMR and HRMS and exhibited excellent inhibitory effects on α-glucosidase. Derivative four exhibited the highest anti-α-glucosidase activity (IC50: 15.71 ± 0.21 μM). Structure-activity relationship results showed that bromine group would be the most beneficial group to anti-α-glucosidase activity. Inhibitory mechnism and inhibition kinetics results showed derivative four was a reversible and mixed-type inhibitor. Molecular docking revealed that derivative four was tightly bind to the amino acid residues of active pocket of α-glucosidase and formed hydrogen bond, π-π stacking, and Pi-Donor hydrogen with α-glucosidase. Moreover, the physicochemical parameters of all derivatives were assessed using SwissADME software. This results also showed that the hybridization of flavonoid and phenylpropionic acid would be a useful strategy for the development of α-glucosidase inhibitors.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jan","modification":"2025-04-05T09:43:13.645Z","creation":"2025-04-05T09:43:13.645Z"},"accession":"S-EPMC9705736","cross_references":{}}