Open AccessMolecular docking studies of deacetylbisacodyl with intestinal sucrase-maltase enzyme
Author(s) -
Ramchander Merugu,
Uttam Kumar Neerudu,
Karunakar Dasa,
Kalpana Virendra Singh
Publication year - 2017
Publication title -
international journal of advances in scientific research
Language(s) - English
Resource type - Journals
ISSN - 2395-3616
DOI - 10.7439/ijasr.v2i12.3821
Subject(s) - docking (animal) , chemistry , hydrogen bond , stereochemistry , ligand (biochemistry) , enzyme , protein–ligand docking , hydrophobic effect , active site , in silico , biochemistry , crystallography , molecule , virtual screening , receptor , organic chemistry , pharmacophore , medicine , nursing , gene
Molecular docking of sucrase-isomaltase with ligand deacetylbisacodyl when subjected to docking analysis using docking server, predicted in-silico result with a free energy of -3.36 Kcal/mol which was agreed well with physiological range for protein-ligand interaction, making bisacodyl probable potent anti-isomaltase molecule. According to docking server Inhibition constant is 5.98Mm. which predicts that the ligand is going to inhibits enzyme and result in a clinically relevant drug interaction with a substrate for the enzyme. Hydrogen bond with bond length 3.45is formed between Pro 64 (A) of target and of ligand, which is again indicative of the docking between target and ligand. Excellent electrostatic interactions of polar, hydrophobic, pi-pi and Van der walls are observed. The proteinligand interaction study showed 6 amino acid residues interaction with the ligand.