Exploring the Inhibitory Potential of CoQ10 on Prenyl transferases through in silico Approach

Prenyltransferases including Farnesyltransferase (FTase) and Geranylgeranyl transferase-I (GGTase-I), play a crucial role in post-translational modifications by facilitating the attachment of isoprenoid groups to specific proteins, thereby influencing their localization and functionality. Dysregulation of these enzymes has been linked to various diseases such as cancer and neurodegenerative conditions. In this study, in order to identify novel anticancer targets, we employed in silico techniques to investigate the inhibitory effects of CoQ10, a naturally occurring compound, on FTase and GGTase-I. We performed molecular docking analyses to assess the binding affinity, stability and interaction profiles of CoQ10 with the active sites of these enzymes. Standard drugs recognized for their inhibitory effects were used as reference compounds for our comparative evaluation. The findings revealed that CoQ10 shows a significant binding affinity and advantageous interaction characteristics with both FTase and GGTase-I, matching or surpassing those of conventional inhibitors. This underscores the potential of CoQ10 as a viable candidate for further exploration as a dual prenyl transferase inhibitor. Additional in vitro and in vivo research are necessary to confirm therapeutic efficacy.