Unlocking E-arylidene Steroid Derivatives as Promising α-Glucosidase Inhibitors
Issued Date
2024-03-05
Resource Type
eISSN
23656549
Scopus ID
2-s2.0-85186230475
Journal Title
ChemistrySelect
Volume
9
Issue
9
Rights Holder(s)
SCOPUS
Bibliographic Citation
ChemistrySelect Vol.9 No.9 (2024)
Suggested Citation
Danova A., Pattanapanyasat K., Kowit, Shigeta Y., Rungrotmongkol T., Hermawati E., Chavasiri Hengphasatporn W. Unlocking E-arylidene Steroid Derivatives as Promising α-Glucosidase Inhibitors. ChemistrySelect Vol.9 No.9 (2024). doi:10.1002/slct.202303887 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/97491
Title
Unlocking E-arylidene Steroid Derivatives as Promising α-Glucosidase Inhibitors
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Corresponding Author(s)
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Abstract
Type 2 diabetes is common and involves α-glucosidase inhibition to regulate glucose. We synthesized twenty E-arylidene steroids with hydroxy and methoxy groups on the aromatic ring. Compounds 3 a, 5 a, 5 b, and 5 d showed notable inhibition, with IC50 values ranging from 1.84±0.28 to 9.25±2.53 μM. Key features for bioactivity include ortho methoxy and α-hydroxy. Various inhibition mechanisms were observed. In silico studies elucidate the possible binding modes of E-arylidene steroids, confirming their enzymatic mechanisms of non/un-competitive inhibitors. Allosteric site 2 emerges as a potential binding site for compounds 3 a, 5 a, and 5 b. Compound 5 d holds promise as a potent α-glucosidase inhibitor compared to acarbose at the orthosteric receptor binding site.