| Literature DB >> 32173438 |
Abdel-Nasser Kawde1, Muhammad Taha2, Raneem Saud Alansari3, Noor Barak Almandil4, El Hassane Anouar5, Nizam Uddin6, Fazal Rahim7, Sridevi Chigurupati8, Muhammad Nawaz9, Shawkat Hayat7, Mohamad Ibrahim4, Praveen Kumar Elakurthy10, Venugopal Vijayan11, Mohamed Morsy12, Hossieny Ibrahim13, Nadeem Baig12, Khalid Mohammed Khan14.
Abstract
α-Glucosidase and α-amylase are enzymes which are associated with diabetic II. These enzymes break macromolecules of sugar into monosugar molecules which is soluble in body, hence increase the sugar level in blood. There is need to develop economical and save inhibitors to prevent them from breaking sugar macromolecules to soluble molecules which will control the level of sugar in blood. Therefore, we synthesized indole-based derivatives (1-18) and evaluated as dual inhibitor for α-glucosidase and α-amylase. These chemical scaffolds were built with variation in aryl ring which were found active with good to moderate activity for α-glucosidase having IC50 value ranging from 13.99 ± 0.10 to 59.09 ± 0.30 μM when compared with standard acarbose with IC50 of 11.29 ± 0.10 μM; for α-amylase IC50 value ranging from 13.14 ± 0.10 to 58.99 ± 0.30 μM when compared with the standard acarbose with IC50 of 11.12 ± 0.10 μM. Structure activity relationship (SAR) has been established for all compounds. Enzymatic kinetic study and molecular docking study have been carried out to investigate the binding interactions α-glucosidase and α-amylase enzyme.Entities:
Keywords: Enzymatic kinetic study; Indole; Molecular docking; α-Amylase; α-Glucosidase
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Year: 2020 PMID: 32173438 DOI: 10.1016/j.ijbiomac.2020.03.090
Source DB: PubMed Journal: Int J Biol Macromol ISSN: 0141-8130 Impact factor: 6.953