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Bioinformation. 2019 Jul 31;15(7):523-529. doi: 10.6026/97320630015523. eCollection 2019.

Design and evaluation of chalconeimine derivatives as α-amylase inhibitors.

Author information

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

Abstract

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.

KEYWORDS:

Molecular docking; alpha-amylase; chalcone; diabetes; hydrazone; hydrogen bond

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