Akt1 is an important macromolecule expressed excessively in many cancers. Inhibition of Akt1 by natural compounds is always advantageous for there are fewer side effects. It is well known that curcumin modifies the behavior of AKT1/AKT2/AKT3 but a natural ligand or its derivative that interacts specifically with AKT1 is one, that will be of tremendous interest in the world of cancers. For the first time, a derivative of curcumin that interacts only with AKT1 but not AKT2 is proposed by way of bioinformatics-based verification studies. Through simulation-based analysis, this research studies the interactions of curcumin derivative with AKT1 protein and compare the same with the fda approved AKT1 inhibitor, capiversatib. The curcumin derivative’s energy was localized along with optimization using the PDB file 4EKL obtained from RCSB. The stability of the curcumin derivative’s non-bonded interactions with the AKT1 protein was studied using Desmond MD method. The affinity of the curcumin derivative’s interaction was -10.327 kcal/mol and for the fda approved molecule, Capivasertib, it was -8.339 kcal/mol. The MMGBSA value of -60.53 kcal/mol for the curcumin derivative-AKT1 complex was much better than the value of -26.65 kcal/mole for the Capivasertib-AKT1 complex. The curcumin derivative molecule did not interact with Akt2 molecule as indicated by the failure of good docking poses by the docking software. The curcumin derivative molecule was helped by hydrogen bond formations with Glu228, Ala230, Lys179, Glu278, Thr312, Tyr315 whereas for Capivasertib, the hydrogen bonds were formed at Glu234, Glu278, Glu228 and Ala230 in addition to various hydrophobic interactions for both the complexes. Molecular dynamics simulation studies confirmed the stability of the curcumin derivative molecule-Akt1 complex for the entire duration of 100 nanoseconds. Hence, the curcumin derivative molecule may target specifically the Akt1 molecule for its behavioural modification.