Journal article
2-Aryl benzimidazoles: Synthesis, In vitro α-amylase inhibitory activity, and molecular docking study


Research Areas
Currently no objects available

Publication Details
Author list: Akande Akinsola Adegboye, Khalid Mohammed Khan, Uzma Salar, Sherifat Adeyinka Aboaba,Kanwal, Sridevi Chigurupati, Itrat Fatima, Mohammad Taha, Abdul Wadood, Jahidul Isalm Mohammad,Huma Khan, Shahnaz Perveen
Publisher: Elsevier
Publication year: 2018
Journal: European Journal of Medicinal Chemistry
Journal name in source: European Journal of Medicinal Chemistry
Volume number: 150
Start page: 248
End page: 260
Number of pages: 13
ISSN: 0223-5234
Web of Science ID: 000430891400018
PubMed ID: 29533872
Scopus ID: 85043359288
eISSN: 1768-3254


Despite of many diverse biological activities exhibited by benzimidazole scaffold, it is rarely explored for the α-amylase inhibitory activity. For that purpose, 2-aryl benzimidazole derivatives 1–45 were synthesized and screened for in vitro α-amylase inhibitory activity. Structures of all synthetic compounds were deduced by various spectroscopic techniques. All compounds revealed inhibition potential with IC50 values of 1.48 ± 0.38–2.99 ± 0.14 μM, when compared to the standard acarbose (IC50 = 1.46 ± 0.26 μM). Limited SAR suggested that the variation in the inhibitory activities of the compounds are the result of different substitutions on aryl ring. In order to rationalize the binding interactions of most active compounds with the active site of α-amylase enzyme, in silico study was conducted.


Projects
Currently no objects available

Keywords
Currently no objects available

Documents
Currently no objects available

Last updated on 2021-12-10 at 08:52