Theoretical investigation of N-trans-cinnamylidene-m-toluidine by DFT method and molecular docking studies

Ancin N. A., Oztas S. G., Kucukterzi O., ALTUNTAŞ ÖZTAŞ N.

JOURNAL OF MOLECULAR STRUCTURE, vol.1198, 2019 (SCI-Expanded) identifier identifier


The structural properties and conformational analysis of N-trans-cinnamylidene-m-toluidine (NTCMT= C16H15N) Schiff base were investigated with experimental and quantum chemical techniques. The molecular geometry of the compound was optimized using density functional theory (DFT), with the B3LYP method combined with the 6-311++ G(d,p) and cc-pVTZ basis sets. The most stable molecular structure of title molecule was obtained by conformational and spectrochemical analysis and compared with its xray data reported previous paper. The theoretical and experimental structural studies on the most stable conformer were carried out by FT-IR, UV-visible, H-1 and C-13 NMR spectroscopic techniques. The calculated vibrational spectra were compared with the experimental spectra and each vibrational wave number was assigned on the basis of potential energy distribution analysis (PED). The global chemical reactivity descriptors of title molecule were determined by using the HOMO and LUMO energy values. The stability of NTCMT arising from hyperconjugative interactions, charge delocalization were obtained using natural bond orbital (NBO) analysis. The Fukui function of atoms were calculated in order to predict the local reactive sites of the title molecule. The molecular electrostatic potential (MEP) surface was simulated to confirm the electrophilic and nucleophilic sites. Neuroprotective nature of the mentioned molecule was also examined by molecular docking analysis. Molecular docking was carried out to introduce the most stable structure of NTCMT molecule into the x-ray crystal structures of acethylcholinesterase to find out the probable binding and interaction mode. The results of molecular docking indicated that the title molecule may display as a good inhibitor against acetylcholinesterase enzyme. (C) 2019 Elsevier B.V. All rights