Primary Author: N. Kirubakaran¹

       Additional Authors:  K. Reeta Vijaya Rani^2, Manoj Govindarajulu⁴, Sindhu Ramesh⁴, Kiruba Mohandoss³, Mohammed Almaghrabi⁴, Timothy Moore⁴, Muralikrishnan Dhanasekaran⁴

1. Siddha Central Research Institute, Chennai – 600 106, Tamilnadu, India.

2. Department of Pharmaceutics, Surya School of Pharmacy, Surya Group of Institutions,

      Vikravandi, Villupuram – 605 652, Tamilnadu, India.

3. Shri Sathya Sai Medical College and Research Institute, Thiruporur, Chengalpet – 603 108,

      Tamilnadu, India.

4. Department of Drug Discovery and Development, Harrison School of Pharmacy, Auburn

      University, Auburn, AL, 36849, USA.

Abstract: 

The objective of the present study was to investigate the effect of Siddha D5 Chooranam on human pancreatic alpha-amylase (1HNY) and alpha-glycosidase (4J5T) by In silco docking studies.  Crystalline structure of the target protein human pancreatic alpha-amylase (1HNY) and alpha-glycosidase (4J5T) was retrieved from protein data bank and protein clean-up process was done and essential missing hydrogen atom were added.  Different orientation of the lead molecules with respect to the target protein was evaluated by Auto dock program.  Ligand Properties of the Compounds like Ascorbic Acid, Epicatechin, Cinnamaldehyde, Linoleic acid, Barbaloin, Costunolide , Cyperol, Mangiferin, Oleanolic acid , Rotundone, Salacinol, Cynaropicirinwere selected for docking studies.  Amino acids such as His 101, Leu 162, Arg 195, Asp 197, Ala 198, Ser 199, Lys 200, His 201, Glu 233, Asp 300 are the core residue involved in mediating the Human pancreatic alpha-amylase (1HNY).  Binding of lead compounds with this core residue may inhibit the enzyme activity.  The compounds Linoleic acid, Cyperol, Magniferin, Rotundone, Salacinol has maximum interactions when compared to that of the standard acarbose. Hence these compounds possess promising human pancreatic alpha-amylase (1HNY) enzyme inhibition activity.  Amino acids such as Asp568, Tyr709, Glu771, Asp392 and Arg428 are the core residue involved in mediating the Human Alpha-Glucosidase (4J5T) enzyme activity.  Binding of lead compounds with this core residue may lead to the enzyme inhibitory activity.   The compounds Epicatechin, Barbolin, Linoleic acid and Costunolide has maximum interactions with when compared to that of the standard acarbose. Hence these compounds of D5 Chooranam possess promising Alpha-Glucosidase enzyme inhibition activity.

Key words: Chooranam, Alpha-Glucosidase enzyme, In silco docking studies