Plk Inhibitors

Rottlerin is an inhibitor that acts against PLK1 (Polo-like kinase 1) and other protein kinases. Its mechanism of action involves direct binding to PLK1, which results in the inhibition of its kinase activity. The disruption of PLK1 activity interferes with the proper execution of mitosis, leading to defects in cell division and potential apoptosis (programmed cell death) in cancer cells.

Wortmannin is a potent inhibitor that targets various kinases, including PLK1 (Polo-like kinase 1). It exerts its inhibitory effect by forming a covalent bond with a conserved lysine residue within the ATP-binding pocket of the kinase. By doing so, Wortmannin irreversibly inhibits PLK1, disrupting its kinase activity and interfering with cell cycle progression. This inhibition can lead to cell cycle arrest and apoptotic cell death.

BI 2536 is a small molecule inhibitor of polo-like kinases (PLKs). Similar to Polo-like Kinase Inhibitor III, BI 2536 works by targeting and inhibiting the activity of PLKs. By inhibiting PLKs, BI 2536 disrupts the normal cell cycle progression, leading to cell cycle arrest and inhibition of cell proliferation.

CID 755673 is an inhibitor designed to specifically target PLK1 (Polo-like kinase 1). It interacts with PLK1 at its ATP-binding site, preventing the kinase from accessing ATP and thus inhibiting its catalytic activity. The disruption of PLK1 function by CID 755673 interferes with mitotic progression, causing defects in cell division and potentially triggering cell death in cancer cells.

BI6727, also known as volasertib, is a selective inhibitor of polo-like kinases (PLKs). Similar to Polo-like Kinase Inhibitor III and BI 2536, BI6727 works by targeting and inhibiting the activity of PLKs. By inhibiting PLKs, BI6727 disrupts the normal cell cycle progression, leading to cell cycle arrest and inhibition of cell proliferation.

Tak-960 is a potent and selective PLK1 (Polo-like kinase 1) inhibitor. It binds to the ATP-binding site of PLK1 and effectively inhibits its catalytic activity. By doing so, Tak-960 disrupts PLK1's function in regulating mitotic processes, leading to cell cycle arrest and apoptosis in cancer cells.

SBE 13 hydrochloride exhibits unique properties as a potent Plk, characterized by its ability to selectively bind to specific protein domains, influencing phosphorylation processes. Its structural conformation allows for enhanced interaction with target kinases, modulating their activity and downstream signaling pathways. The compound's solubility in aqueous environments facilitates rapid cellular uptake, while its reactivity with nucleophiles underscores its role in dynamic cellular processes and regulatory mechanisms.

ON-01910 (also known as rigosertib) is a small molecule that works by interfering with PLK1. It aims to disrupt cancer cell proliferation and induce cell death (apoptosis) in cancer cells.

Cyclapolin 9 functions as a distinctive Plk, showcasing remarkable selectivity in its interaction with cellular substrates. Its unique molecular architecture promotes specific binding to regulatory motifs, thereby influencing critical phosphorylation events. The compound's kinetic profile reveals a rapid association and dissociation with target proteins, enhancing its modulatory effects on signaling cascades. Additionally, its reactivity with electrophiles highlights its involvement in intricate cellular regulatory networks.

BTO-1 exhibits unique properties as a Plk, characterized by its ability to engage in selective protein-protein interactions that modulate cell cycle progression. Its structural features facilitate the formation of stable complexes with key mitotic regulators, leading to enhanced phosphorylation efficiency. The compound demonstrates a distinctive reaction kinetics profile, with a notable propensity for rapid conformational changes that amplify its regulatory impact on cellular pathways. Furthermore, BTO-1's reactivity with specific nucleophiles underscores its role in fine-tuning cellular signaling dynamics.