H2-A Inhibitors

H2-A inhibitors, in the context of this table, refer to a class of compounds that modulate the function of histones by altering their post-translational modifications, particularly acetylation. Histone acetylation is a key epigenetic marker that affects the accessibility of chromatin and thereby regulates gene expression. The compounds listed are primarily inhibitors of histone deacetylases (HDACs). HDACs are enzymes that remove acetyl groups from histones, leading to a closed chromatin conformation and reduced gene expression. Inhibition of HDACs by the compounds listed results in an increase in acetylation levels of histones, including H2A, assuming H2-A refers to H2A. This hyperacetylation leads to an open chromatin structure, which can increase the transcription of certain genes.

The HDAC inhibitors listed above are structurally diverse compounds that share the functional property of inhibiting the deacetylase activity of HDAC enzymes. Trichostatin A, Vorinostat, and similar compounds bind to the active site of HDACs, blocking their enzymatic activity. This binding results in an accumulation of acetylated histones, including H2A, which can lead to changes in gene expression patterns within cells. The specificity and potency of these inhibitors vary, with some like Panobinostat and Romidepsin being more potent and others like Valproic acid being less selective. The overall effect of these inhibitors on histones is to maintain a state of hyperacetylation, which is generally associated with an active chromatin state and potentially increased gene expression. The exact mechanism of action of each HDAC inhibitor can differ based on their chemical structure, which determines their affinity, selectivity, and ability to penetrate the cell and reach the nucleus where histones reside.