1st International and 10th National Iranian Conference on Bioinformatics
Home Accepted Papers
Synthesis and in silico docking studies of curcumin-polyhydroxy derivatives as novel dual inhibitors of α-amylase and α-glucosidase
Paper ID : 1423-ICB10
Authors:
Pedram Routabi *1, Maryam Mehrabi2, Reza Khodarahmi3, Hadi Adibi4, Masomeh Mehrabi3
1Department of biology, Faculty of Sciences, Razi University, Kermanshah, Iran
2Department of Biology, Faculty of Sciences, Razi University, Kermanshah, Iran
3Medical Biology Research Center, Health Technology Institute, Kermanshah University of Medical Sciences, Kermanshah, Iran
4Pharmaceutical Sciences Research Center, Health Institute, Kermanshah University of Medical Sciences, Kermanshah, Iran
Abstract:
Over the past twenty years, the prevalence of diabetes as one of the most common metabolic diseases has become a public health problem worldwide [1]. Blood glucose control is an important factor in delaying the onset and progression of diabetes-related complications [2]. Therefore, in this study, curcumin- polyhydroxy derivatives were synthesized and used as effective agents in the treatment of diabetes with inhibitory properties against two carbohydrate-hydrolyzing enzymes α-glucosidase (α-Glu) and α-amylase (α-Amy) which are known to be significant therapeutic targets for the reduction of postprandial hyperglycemia [3]. In search of potent dual inhibitors of α-Amy and α-Glu, we have synthesized curcumin-polyhydroxy derivatives, characterized by FTIR and MS then the binding interaction details of compounds to α-Amy and α-Glu were determined using a molecular docking study. Molecular docking was performed using AutoDock Vina and docking results were analyzed by PyMOL v.2.3.2.1 and LigPlot+ v.1.4.2 software. Molecular docking indicated that curcumin derivatives mainly interacted with amino acid residues located in the active site of α-Amy and α-Glu. The binding energies obtained from the docking of α-Amy with curcumin (C1), C2, C3, and C4 derivatives were -8.4, -8.2, -8.5 and -8.7, kcal/mol, respectively. Also, C1, C2, C3, and C4 derivatives showed binding energies of -7.6, -7.8, -8.0 and -8.0 kcal/mol in communication with the active site of α-Glu, respectively. This study indicated that curcumin-polyhydroxy derivatives could occupy the active catalytic site of α-Amy and α-Glu, resulting in the inhibitory effect due to steric hindrance, but more preclinical and clinical studies should be carried out in the future.
Keywords:
Curcumin-based derivatives, Anti-diabetic, α-Amylase, α-Glucosidase, Molecular docking
Status : Paper Accepted (Poster Presentation)