Several studies have linked Quinone Reductase 2 to the generation of quinone free radicals, several neuronal degenerative diseases, and cancer. There is no definitive correlation between traditionally obtained MT3 ligand affinity and hQR2 inhibition exists limiting the understanding of how these ligands are accommodated in the hQR2 active site. Based on these outlooks we have tried to identify novel target using target search option in zinc database to explore probable reason for affinity and inhibition of Quinone Reductase 2 using docking studies. The docking analysis divulge that compound zinc_6182368 inhibit quinone reductase 2 via hydrogen bonding, arene-arene interaction by acquiring different enantiomeric forms in the active site of receptor. The analysis divulge that compound zinc_6182368 bind to the quinone reductase in a stereoselective manner, existence of chiral centre is essential to acquire bioactive conformation within the active site while arene-arene interaction may enhance binding affinity of ligand towards receptor surface.
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