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Design and evaluation of chalconeimine derivatives as α-amylase inhibitors


Prithivirajan Balu1, Jebastin Sonia Jas1,2 & Marimuthu Govindaraj3,*



1Research and Development Centre, Bharathiar University, Coimbatore-641046, India; 2Department of Chemistry, IFET College of Engineering, Villupuram-605108, India; 3Department of Chemistry, Swami Dayananda College of Arts and Science, Manjakkudi-612610, Tiruvarur District, India;


Marimuthu Govindaraj - *Corresponding author: E-mail: gmarimuuthu@gmail.com


Article Type

Research Article



Received July 16, 2019; Accepted July 28, 2019; Published July 31, 2019



Alpha-amylase is a known target for type II diabetes. Therefore, it is of interest to design α-amylase inhibitors based on hydrazone scaffold. The structure of these hybrids was confirmed by spectroscopic analysis (IR, 1H-and 13C NMR). All the compounds have potential inhibitory properties as shown by in vitro α-amylase inhibition activity. The compound 5-((1Z,3Z)-3-(benzo[d][1,3]dioxol-5-yl)-3-((2-chloropyridin-3-yl)imino)prop-1-en-1-yl)-2-(difluoromethoxy)phenol(4a) in 100 μg/mL concentration showed a high inhibition of 85.23%. In vitro α-amylase inhibition was further supported by docking studies of compound against the active site of pig pancreatic α-amylase (PDB ID: 3L2M).
Docking studies revealed that the bonding interactions found between the compound and human pancreatic α-amylase are similar to those responsible for α-amylase inhibition by acarbose.



Molecular docking, diabetes, alpha-amylase, hydrogen bond, hydrazone, chalcone.



Balu et al. Bioinformation 15(7): 523-529 (2019)


Edited by

P Kangueane






Biomedical Informatics



This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.