Molecular docking studies on fluoro-substituted chalcones as potential DprE1 enzyme inhibitors

Abstract

In this study, docking studies were performed on a series of fluoro-substituted chalcones (E1–E7, Z1-Z7, H1–H7) with DprE1 enzyme inhibition activities. The results showed that both the positions of the substituents and the type of chalcones seemed to be critical for their inhibition against DprE1. Chalcone derivatives exhibited binding affinity values of < −8.0 kcal/mol. The compounds E6, E7, and Z7 having a double bond in the linker group were effective inhibitors and it were found that this structural motif had an influence on the binding profile of molecules. The best docking results were detected for Z7, which is the cis-isomer of E7 from the E group. The SAR results of the novel DprE1 inhibitors were revealed in this study and the inhibitors were predicted to have excellent potencies from the developed models. The results could greatly contribute toward designing potential new DprE1 inhibitors with better activities.