TY - JOUR
T1 - Computational study of geometry, polarizability, hyperpolarizability and molecular docking studies of naproxen
AU - Aktar, Sharmin
AU - Khan, Mohammad Firoz
AU - Rahman, Muhammed Mahfuzur
AU - Rashid, Mohammad A.
N1 - Publisher Copyright:
© 2016, University of Dhaka. All rights reserved.
PY - 2016
Y1 - 2016
N2 - 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.
AB - 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.
KW - Geometry
KW - Molecular docking
KW - Naproxen
KW - Polarizibility
UR - http://www.scopus.com/inward/record.url?scp=84983027554&partnerID=8YFLogxK
U2 - 10.3329/dujps.v15i1.29191
DO - 10.3329/dujps.v15i1.29191
M3 - Article
AN - SCOPUS:84983027554
SN - 1816-1820
VL - 15
SP - 37
EP - 45
JO - Dhaka University Journal of Pharmaceutical Sciences
JF - Dhaka University Journal of Pharmaceutical Sciences
IS - 1
ER -