Abstract
Objective: In addition to its role in the formation mechanism of inflammation, the binding potential of COX inhibitors, which can inhibit tumorogenesis by induce apoptosis, has been explored by molecular docking studies on wild-type RAS enzyme.
Material and Method: KRAS enzyme (PDB ID: 4OBE), which consists is obtained by the x-ray crystallization method, was chosed considering the resolution. The 2D structures of ligand molecules were drawn in the ChemDraw 19.1. The MOE 2020 program was used to form the docking studies.
Result and Discussion: As a result of docking studies, it has been understood that the presence of aromatic structures in 3a and 3b ligand molecules is critical for ligand-receptor interaction. it has been understood that there must be a certain distance between the carbonyl group and the nonpolar part of the molecule for the molecule to bind to the receptor site with a high affinity. In the following stages, more effective anticancer drug molecules can be obtained by design molecules with an appropriate diameter and length, having functional groups containing the suitable electron donor or acceptor.