Identification of new structure of indol-3-acetyl-arylsulfonohydrazide as potent α-glucosidase and α-amylase inhibitors and molecular docking

• Published in: Journal of Molecular Structure
• Main Author: Taha M.; Rahim F.; zaman K.; Imran S.; Khan K.M.; Shah S.A.A.; Uddin N.
• Format: Article
• Language: English
• Published: Elsevier B.V. 2025
• Online Access: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85209591318&doi=10.1016%2fj.molstruc.2024.140719&partnerID=40&md5=013b2862aab435f98890306f743723cf

Herein this work, indole analogs (1–16) were synthesized by treating 2-(1H-indol-3-yl)acetohydrazide with various aryl sulfonyl chloride in pyridine as solvent and screened for α-amylase and α-glucosidase inhibitory activity under positive control of standard drug acarbose (IC50 = 12.80 ± 0.10 μM /12.90 ± 0.10 μM. All analogs of the series appeared with excellent to good inhibitory activity as compared to standard drug. The inhibitory activity range for α-amylase is 0.70 ± 0.01 μM to 19.40 ± 0.40 μM, while for α-glucosidase inhibitory activity is 1.20 ± 0.10 μM to 20.40 ± 0.40 μM respectively. Most of the analogs appeared with excellent inhibitory activity, and some analogs like 5, 6, 7, 8, 9, 10,13 and 14 for both enzymes displayed many folds better inhibitory activity than standard drug acarbose. The influences of substituents on inhibitory activity were superficially resonated via structure activity relationship. Docking studies were established to confirm the binding interaction between analogs and active sites of enzymes. © 2024 Elsevier B.V.