Open AccessComputational Study of Geometry, Polarizability, Hyperpolarizability and Molecular Docking Studies of Naproxen
Author(s) -
Sharmin Aktar,
Mohammad Firoz Khan,
Muhammed Mahfuzur Rahman,
Mohammad A. Rashid
Publication year - 2016
Publication title -
the dhaka university journal of pharmaceutical sciences
Language(s) - English
Resource type - Journals
eISSN - 1816-1839
pISSN - 1816-1820
DOI - 10.3329/dujps.v15i1.29191
Subject(s) - hyperpolarizability , polarizability , polarizable continuum model , chemistry , hydrogen bond , computational chemistry , molecular geometry , docking (animal) , naproxen , bond length , mulliken population analysis , molecule , density functional theory , crystallography , stereochemistry , solvation , organic chemistry , medicine , alternative medicine , nursing , pathology
A computational assessment of geometry, molecular electrostatic potential (MESP), Mulliken charge distribution, polarizability, hyperpolarizability and molecular docking study of naproxen with human COX-2 enzyme were conducted. B3LYP level of theory using 6-31G(d,p) basis set was used to optimize the structure of naproxen. The default Polarizable Continuum Model (PCM) of Gaussian09 software was applied for all calculations involving solvents, water and n-octanol. Almost all bond lengths and angles of naproxen agree very well with the X-ray crystal structure suggesting that the molecule is well described with B3LYP/6-31G(d,p) level of theory. The polarizability and first order hyperpolarizability were increased with the increase of solvent polarity. Moreover, docking study revealed that naproxen interacts with human COX-2 enzyme at a binding affinity of -8.2 kcal/mol forming one hydrogen bond with TYR354.Dhaka Univ. J. Pharm. Sci. 15(1): 37-45, 2016 (June)