RETRACTED ARTICLE: Synthesis, molecular docking and molecular dynamics simulation of 1,4-bis(4,5-diphenyl-1H-imidazol-2-yl) benzene as a potential inhibitor against LDHA

Lactate dehydrogenase is one of the major enzymes for the anaerobic metabolic pathway. It belongs to the oxidoreductases class and is responsible for converting pyruvate to lactate in the final step of glycolysis. It has been reported that this step is elevated in many types of cancers. Compared to normal cells, one of the most prominent characteristics of tumor cells is that the metabolic energy switches from oxidative phosphorylation to increased glycolysis rate. A new 2,4,5 trisubstituted imidazole derivative 1,4-bis(4,5-diphenyl-1H-imidazole-2-yl) benzene has been synthesized by one-pot reaction. Spectral techniques like FTIR, 1HNMR and 13CNMR characterize the product. The synthesized compound is virtually investigated as a potential LDHA inhibitor. The results from computational modeling show that the imidazole derivative inhibited LDHA. The molecular docking confirmed the binding of the ligand with a docking score of −10.6 kcal/mol. Molecular dynamics simulation of 100 ns is used to examine the stability of the docked complex. The RMSD graph confirms the stability throughout the simulated time.