Abstract

The assessment of histone deacetylases in conjunction with curcumin, conducted through the Mcule Database employing the Autodock Vina algorithm, involves an examination of molecular interactions. This analysis includes the calculation of binding energies, revealing the strength and stability of the interactions between curcumin and various histone deacetylase targets. The comparison encompasses diverse aspects such as binding energies, specific binding sites, interactions across different targets, structural details, and potential implications for biological activity. The results imply that curcumin shows heightened affinity for histone deacetylase 4 in comparison to other investigated histone deacetylases.

Keywords: HDACs, Curcumin, Molecular docking