Synthesis of alpha amylase inhibitors based on privileged indole scaffold

• Published in: Bioorganic Chemistry
• Main Author: Noreen T.; Taha M.; Imran S.; Chigurupati S.; Rahim F.; Selvaraj M.; Ismail N.H.; Mohammad J.I.; Ullah H.; javid M.T.; Nawaz F.; Irshad M.; Ali M.
• Format: Article
• Language: English
• Published: Academic Press Inc. 2017
• Online Access: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85018732634&doi=10.1016%2fj.bioorg.2017.04.010&partnerID=40&md5=c1e0613a6e04e30e2cf7fbb9284b98e3
• ISSN: 452068
• DOI: 10.1016/j.bioorg.2017.04.010

Twenty five derivatives of indole carbohydrazide (1–25) had been synthesized. These compounds were characterized using 1H NMR and EI-MS, and further evaluated for their α-amylase inhibitory potential. The analogs (1–25) showed varying degree of α-amylase inhibitory potential. ranging between 9.28 and 599.0 µM when compared with standard acarbose having IC50 value 8.78 ± 0.16 µM. Six analogs, 25 (IC50 = 9.28 ± 0.153 µM), 22 (IC50 = 9.79 ± 0.43 µM), 4 (IC50 = 11.08 ± 0.357 µM), 1 (IC50 = 12.65 ± 0.169 µM), 8 (IC50 = 21.37 ± 0.07 µM) and 14 (IC50 = 43.21 ± 0.14 µM) showed potent α-amylase inhibition as compared to the standard acarbose (IC50 = 8.78 ± 0.16 µM). All other analogs displayed good to moderate inhibitory potential. Structure-activity relationship was established through the interaction of the active compounds with enzyme active site with the help of docking studies. © 2017 Elsevier Inc.