Abstract

Lipoxygenase are a group of enzymes that are involved in fatty acid oxidation in plant, animal and mammalian
cells. All lipoxygenases are known to be pharmaceutically important, seen to mediate inflammatory and cancer
disorders. In this study, the homology modeling methodology is used to model the human 15-Lox which plays an
important pathological role in all types of cancer. Based on NCBI blast search a template protein 1-lox was
chosen with whom the target protein sequence identity was seen to be 81%. The target protein modeled using
the modeller 9v9 program; followed by refinement through energy minimization processes and validated by
saves server. Analysis of the Ramachandran plot shows 99.98% amino acids fall in the allowed region,
illustrating the model structure to be accurate. The modelled protein was docked with the seven ligand
compound using the schrödinger maestro 9.2 tool and results showed the masoprocol and NDGA legend have
good interactions. Both masoprocol and NDGA ligands are conformers and bind with the same amino acid in
the binding site of the modeled protein. The docking score for masoprocol was -7.53, and for NDGA -7.12 with
the modeled protein. Both the docked protein ligand complexes were refined and stabilized by molecular
dynamic simulation in Desmond's. The simulation results, potential energy and RMSD graph showed the
protein-ligand complexes are stabilized at 3nsec.