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Most of the biological testing of α-glucosidase inhibitors was carried out on yeast and rat intestinal. The aim of this study was to explore molecular interactions which occurred during inhibition process of human-neutral α-glucosidase by cinnamic acid derivatives. In this paper, cinnamic acid was used as the lead compound whose carboxylic acid moeity was replaced by alkyl amine against the macromolecule target which was human-neutral α-glucosidase enzyme. In order to understand the mechanism of interaction of the ligand binding conformations and to identify potent α-glucosidase inhibitor, molecular modeling studies with homology modeling method were used to investigate the problem. The structure of homology model of human α-glucosidase was built by using neutral-human α-glucosidase (GANC) with 914 amino acid residues from the Swiss-Prot with Q8TET4 identity and using the mold template of 2G3M (PDB ID). The model of enzyme was constructed based on the crystal structure of the S.solphataricus α-glucosidase, Ma1A, and human N-terminal subunit of Maltase Glucoamylase (NtMGAM). The molecular docking simulation of cinnamic acid derivatives was carried out on Autodock 4.2. Two parameters from docking simulation that can predict the inhibition activity of α-glucosidase enzyme are: low free energy Gibs and low kinetic inhibition value. The Gibs free energy value (ΔG) obtained from the docking simulation showed that 13 cinnamic acid derivatives compounds had an affinity for the receptor α-glucosidase. These compound could act as α-glucosidase inhibitor.

Design of Cinnamic Acid Derivatives and Molecular Docking Toward Human-Neutral a-Glucosidase by using Homology Modeling