Quantum chemical calculation,topological analysis,biological evaluation and molecular docking of allo-ocimenol against breast cancer

The main aim of this study is to identify the structural stability of allo-ocimenol and its molecular reactivity against breast cancer-associated proteins to confirm its anti-cancer capability using density function theory and molecular docking analysis. The structural optimization was carried out via the DFT/B3LYP technique with a 6-311++G (d,p) basis set. The molecular geometry and vibrational assignments of the Allo-Ocimenol molecule were analyzed through density functional theory (DFT). Through optimized molecular structure, the vibrational frequencies (FT-IR and FT-Raman) were assigned and related with experimentally observed vibrational frequencies and the UV spectrum was computed and experimentally confirmed. The allo-ocimenol's reactive activity was further analyzed through a computed molecular electrostatic potential surface. Utilizing the HOMO-LUMO energies and molecular electrostatic potential energy gap, the reactivity and molecular stability of the allo-ocimenol molecule was calculated. Mulliken and natural population analyses were used to determine the charge distribution across the allo-ocimenol atoms. The natural bond orbitals were used to demonstrate the bioactivity of the titled molecule. RDG evaluation was used to examine the weak interactions of the allo-ocimenol molecule. ELF and LOL analyses were utilized to investigate the topology of the allo-ocimenol molecule. Thermodynamic evaluation has been utilized to acquire values and asses the thermodynamic parameters that reveal the thermal stability of the title molecule. Allo-Ocimenol's anti-microbial activity was assessed through an in-vitro disc diffusion method, and its tumor inhibitory and pharmacokinetic properties were evaluated through an in-silico approach using molecular docking and ADMET investigation. Zones of clearance were seen in anti-microbial analyses at various concentrations, and the breast cancer target protein NAMPT established the greatest binding potential, with a docking value of −7.4 Kcal mol⁻¹.