A novel coronavirus disease (COVID-19) caused by SARS-CoV2 has now spread globally . Replication/transcription machinery of this virus consists of RNA-dependent RNA polymerase (nsp12 or RdRp) and its two cofactors nsp7 and nsp8 proteins . Hence, RdRp has emerged as a promising target to control COVID-19 . In the present study, we are reporting a novel inhibitor VTRM1.1 against the RdRp protein of SARS CoV2 . A series of antivirals were tested for binding to the catalytic residues of the active site of RdRp protein . In-silico screening, molecular mechanics, molecular dynamics simulation (MDS) analysis suggest ribavirin, and remdesivir have good interaction with the binding site of the RdRp protein as compared to other antiviral investigated . Hence, ribavirin and remdesivir were used for the denovo fragments based antiviral design . This design, along with docking and MDS analysis, identified a novel inhibitor VTRM1 that has better interaction with RdRp as compared to their parent molecules . Further, to produce a lead-like compound, retrosynthetic analysis, and combinatorial synthesis were performed, which produces 1000 analogs of VTRM1 . These analogs were analysed by docking and MDS analysis that identified VTRM1.1 as a possible lead to inhibit RdRp protein . This inhibitor has a good docking score (−7.24 kcal/mol) and favourable binding energy (−79.88 kcal/mol) than remdesivir (−6.038; −72.07 kcal/mol) and bind at catalytic AS760 and Asp761 of the active site . The VTRM1.1 also interacts with RdRp in the presence of RNA primer and other cofactors . It was also seen that, VTRM1.1 do not have off-target in human . Therefore, the present study suggests a hybrid inhibitor VTRM1.1 for the RNA-dependent RNA polymerase of SARS CoV2 that may be useful to control infection caused by COVID-19.