Abstract
The Ciproxifan was docked into the active site of histamine N- methyl transferase (HNMT) enzyme and evaluated, based on fitness scoring function A Score available in the Argus lab software. We observed that the A Score correlated well with least binding energy. Such as most active compound Ciproxifan that binds the HNMT enzyme with high of GA Score of –8.04804 K.cal/mole. These results indicate that the GA Score is a better parameter to assess the binding of Ciproxifan analogue as inhibitor of HNMT enzyme. To optimize and calculate the structure of Histamine H3 receptor antagonist drug , Ciproxifan. Docking of Ciproxifan into the active site of protein PDB ID: 2AOT showed that two hydrogen bonds formed with carbonyl group of ligand with hydroxyl group of Tyrosine (Tyr) 147 and amide group of Glutamine (Gln) 94 . The best scoring function (binding affinity) was found to be -8.04804 K.cal/mol. Descriptive Statistical Scoring Function. The non-bonded potential energies were computed for Ciproxifan, which is the H3 receptor antagonist and sedative psychoactive in nature. In the present calculation all the possible pairs of non – bonded interaction have been included for the energy calculation. For the present study, one crystal structure of receptor protein (2AOT) was used to validity A Score scoring function. Docking results were analyzed by Argus Lab software. Docking of Anta 16 into the active site of protein 2AOT showed that two hydrogen bonds formed with carbonyl group of ligand with hydroxyl group of Tyr 147 and amide group of Gln 94. The hydrophobic amino acid residues Gln 94,Gln 143,Glu 89, Gly 60, Gly 61,Gly 62, His 29, Ile 66,Ile 142, Met 144, Pro 90, Ser 91,ser 120,Thr 119, Tyr 147 presents as binding site. The best scoring function (binding affinity) was found to be -8.04804 K.cal/mol.
