Abstract
Histone deacetylase (HDAC2) belongs to the hydrolase family and a promising target for cancers. We reported 96 hydroxamic compounds optimized using hydrogen-donors, hydrophobic and electron withdrawing groups followed by molecular docking studies. The optimized compounds show good LibDock score and H-bond interaction in the active site of HDAC2. We selected 20 compounds as the best HDAC2 inhibitors based on the LibDock score, binding energy and hydrogen bonding. ADMET predictions on these compounds show good absorption, BBB penetration and no liver toxicity. We subsequently report four compounds selected as best HDAC2 inhibitors based on the LibDock, binding energy, H-bonding and ADMET properties.
Highlights
Chromatin structure of histone has two forms such as Histone acetylases (HATs) and Histone deacetylases (HDACs)
The acetylation status of histone operated by histone acetylases and histone deacetylases, which are in equilibrium [1].The main function of HDAC is deacetylation of ε-amino groups of lysine located near the amino terminal of core histone proteins and restore positive charge on lysine residue, which results in tightening of nucleosome structure and gene silencing [2]
Based on molecular docking and H-bond interaction four compounds are selected as best inhibitor of histone deacetylases 2 (HDAC2) protein
Summary
Chromatin structure of histone has two forms such as Histone acetylases (HATs) and Histone deacetylases (HDACs). The acetylation status of histone operated by histone acetylases and histone deacetylases, which are in equilibrium [1].The main function of HDAC is deacetylation of ε-amino groups of lysine located near the amino terminal of core histone proteins and restore positive charge on lysine residue, which results in tightening of nucleosome structure and gene silencing [2]. HDACs deacetylate the histone proteins, and deacetylate non-histone proteins, such as p53 and GATA-1 [3].
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