Histone deacetylase (HDAC) has a critical function in regulating gene expression. The inhibition of HDAC has developed as an\ninteresting anticancer research area that targets biological processes such as cell cycle, apoptosis, and cell differentiation. In this\nstudy, an HDAC inhibitor that is available commercially, suberoyl anilide hydroxamic acid (SAHA), has been modified to improve\nits efficacy and reduce the side effects of the compound. Hydrophobic cap and zinc-binding group of these compounds were\nsubstituted with boron-based compounds, whereas the linker region was substituted with p-aminobenzoic acid. The molecular\ndocking analysis resulted in 8 ligands with ?G binding value more negative than the standards, SAHA and trichostatin A (TSA). That\nligands were analyzed based on the nature of QSAR, pharmacological properties, and ADME-Tox. It is conducted to obtain a potent\ninhibitor of HDAC class II Homo sapiens.The screening process result gave one best ligand, Nova2 (513246-99-6), which was then\nfurther studied by molecular dynamics simulations.
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