Author(s)

Khalid El Akri, Rokaya Mouhibi, Mohamed Zahouily, Naîma Hanafi, Moulay Abdellah Bahlaoui

Materials, Catalysis and Valorization of Natural Resources Laboratory (URAC 24), Faculty of Sciences and Techniques,Hassan II University, Mohammedia, Morocco.
Materials, Catalysis and Valorization of Natural Resources Laboratory (URAC 24), Faculty of Sciences and Techniques,Hassan II University, Mohammedia, Morocco; Organic Chemistry, Catalysis and Environment Laboratory, Faculty of Sciences,Hassan II University, Casablanca, Marocco.
Organic Chemistry, Catalysis and Environment Laboratory, Faculty of Sciences,Hassan II University, Casablanca, Marocco.

A series of N-carbonyl-functionalized ureas, carbamates and thiocarbamates derivatives (or N-Chloro sulfonyl isocyanate
“N-CSI”) were involved in linear and nonlinear physicochemical quantitative structure-activity relationship
“QSAR” analysis to find out the structural keys to control the inhibition against Sterol O-Acyl-Transferase-1 “SOAT-1”.
The results indicate the important effects of geometrical and chemical descriptors on the inhibitory activity of SOAT-1.
The molecules were also screened for three-dimensional molecular docking on the crystal structure of ACAT-1 (1WL5
for ACAT-1, PDB). A comparison between 2D-QSAR and 3D molecular docking studies shows that the latter confirm
the first results and represent a good prediction of the chemical and physical nature of interactions between our drug
molecules and enzyme SOAT-1.

Sterol O-Acyl-Transferase-1; N-CSI Analogs; QSAR; MLR; ANN; 3D Molecular Docking

K. Akri, R. Mouhibi, M. Zahouily, N. Hanafi and M. Bahlaoui, "Physicochemical 2D-Qsar and 3D Molecular Docking Studies on N-Chlorosulfonyl Isocyanate Analogs as Sterol O-Acyl-Transferase-1 “Soat-1” Inhibitors," Open Journal of Medicinal Chemistry, Vol. 3 No. 4, 2013, pp. 100-120. doi: 10.4236/ojmc.2013.34013.