Journal article
Exploring efficacy of indole-based dual inhibitors for α-glucosidase and α-amylase enzymes: In silico, biochemical and kinetic studies

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Publication Details
Author list: Abdel-Nasser Kawde, Muhammad Taha, Raneem Saud Alansari, Noor Barak Almandil, El Hassane Anouar, Nizam Uddin, Fazal Rahim, Sridevi Chigurupati, Muhammad Nawaz, Shawkat Hayat, Mohamad Ibrahim, Praveen Kumar Elakurthy, Venugopal Vijayan, Mohamed Morsy, Hossieny Ibrahim, Nadeem Baig and Khalid Mohammed Khan
Publisher: Elsevier
Publication year: 2020
Journal: International Journal of Biological Macromolecules
Volume number: 154
Issue number: 1 July 2020
Start page: 217
End page: 232
Number of pages: 16
ISSN: 0141-8130
Web of Science ID:
PubMed ID:
Scopus ID: 85081729713
eISSN: 1879-0003

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.

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Last updated on 2020-26-03 at 14:43