G9a Inhibitors

Chaetocin is a potent inhibitor of G9a, a histone methyltransferase involved in epigenetic regulation. It selectively binds to the enzyme's active site, disrupting its interaction with histone substrates and altering chromatin structure. This interference leads to changes in gene expression profiles, impacting cellular differentiation and proliferation. Chaetocin's unique molecular interactions and specificity highlight its role in modulating epigenetic landscapes, making it a significant compound in the study of gene regulation.

BIX01294 hydrochloride is a selective inhibitor of G9a, a key histone methyltransferase that plays a crucial role in the methylation of lysine residues on histone proteins. Its unique binding affinity allows it to effectively disrupt the enzyme's catalytic activity, leading to altered histone modifications and subsequent changes in chromatin dynamics. This compound's distinct interaction with G9a influences epigenetic regulation, providing insights into the mechanisms of gene expression modulation.

Histone Lysine Methyltransferase Inhibitor, targeting G9a, exhibits a high specificity for the enzyme's active site, effectively blocking its methyltransferase activity. This inhibition alters the methylation landscape of histones, impacting chromatin structure and accessibility. The compound's kinetic profile reveals a competitive inhibition mechanism, where it competes with the natural substrate, leading to significant alterations in gene regulatory networks and epigenetic modifications.

UNC 0224 is a selective inhibitor of G9a, demonstrating a unique binding affinity that stabilizes the enzyme in an inactive conformation. This compound disrupts the enzyme's catalytic cycle, influencing the dynamics of histone modification. Its interaction with G9a alters the conformational landscape, resulting in a profound impact on chromatin remodeling. The compound's distinct molecular interactions facilitate a nuanced modulation of epigenetic regulation, underscoring its role in cellular processes.

UNC0638 is a potent G9a inhibitor that displays high selectivity over other histone methyltransferases, reducing H3K9me2 levels and reactivating silenced genes.

UNC 0646 serves as a selective inhibitor of G9a, exhibiting a unique mechanism of action through its ability to form stable complexes with the enzyme. This interaction hinders the transfer of methyl groups to histone substrates, effectively altering the enzyme's kinetic profile. By modulating the enzyme's active site dynamics, UNC 0646 influences downstream signaling pathways and chromatin accessibility, thereby impacting gene expression patterns and cellular behavior.

UNC 0642 is a selective G9a inhibitor that disrupts the enzyme's catalytic activity by binding to its active site, leading to a conformational change that impedes substrate recognition. This compound exhibits a high affinity for G9a, resulting in altered reaction kinetics and a significant reduction in histone methylation. Its unique binding dynamics can influence chromatin structure and stability, thereby affecting transcriptional regulation and cellular processes.

A-366 selectively inhibits G9a, leading to a decrease in H3K9me2 levels, potentially affecting gene expression and cellular processes regulated by G9a.

UNC0631 is a potent inhibitor of G9a, characterized by its ability to form stable interactions with the enzyme's active site. This compound induces a distinct conformational shift, which not only hinders substrate access but also alters the enzyme's overall dynamics. By modulating the enzyme's activity, UNC0631 impacts the methylation landscape of histones, thereby influencing epigenetic regulation and chromatin remodeling processes within the cell.

EPZ005687 is a potent and selective inhibitor of G9a, leading to a reduction in H3K9me2 levels and showing promise in modulating chromatin-related processes.