p35 Inhibitors

A natural product that inhibits multiple CDKs, including CDK5.

(R)-DRF053 acts as a p35 inhibitor, distinguished by its capacity to disrupt cyclin-dependent kinase interactions. The compound features a chiral center that influences its binding affinity and selectivity towards target proteins. Its unique steric configuration facilitates specific molecular recognition, while the presence of functional groups enhances solubility and reactivity. This results in altered reaction kinetics, providing insights into regulatory mechanisms within cellular pathways.

Indirubin-5-sulfonic acid sodium salt functions as a p35 inhibitor, characterized by its ability to modulate protein-protein interactions through specific hydrogen bonding and electrostatic interactions. Its sulfonic acid group enhances water solubility, promoting efficient diffusion in biological systems. The compound's unique structural features allow for selective binding to target kinases, influencing downstream signaling pathways and altering cellular dynamics. Its kinetic profile reveals distinct reaction rates, contributing to a deeper understanding of regulatory networks.

A broad-spectrum inhibitor of multiple CDKs, including CDK5.

PNU 112455A hydrochloride acts as a p35 inhibitor, distinguished by its capacity to disrupt enzyme-substrate interactions via hydrophobic and ionic interactions. The presence of the hydrochloride moiety enhances its stability and solubility in polar environments, facilitating its engagement with target proteins. This compound exhibits unique conformational flexibility, allowing it to adapt to various binding sites, thereby influencing cellular signaling cascades and modulating regulatory mechanisms. Its reaction kinetics suggest a rapid association and dissociation profile, providing insights into its dynamic role in biochemical pathways.

Cdk1/5 Inhibitor functions as a p35 inhibitor, characterized by its ability to selectively bind to cyclin-dependent kinases through a combination of hydrogen bonding and van der Waals forces. This compound exhibits a unique structural motif that promotes specificity in target recognition, influencing downstream signaling pathways. Its kinetic properties reveal a notable affinity for target enzymes, leading to effective modulation of cell cycle progression and regulatory networks.

A potent CDK1/2/5/9 inhibitor that blocks CDK5 function.

Hymenidin, as a p35 inhibitor, showcases a distinctive ability to interact with cyclin-dependent kinases via hydrophobic interactions and electrostatic forces. Its unique conformation facilitates precise binding, altering enzyme dynamics and impacting cellular signaling cascades. The compound's reaction kinetics indicate a rapid association with target proteins, enhancing its regulatory influence on cellular processes. This specificity underscores its role in modulating kinase activity and related pathways.

N9-Isopropyl-olomoucine, functioning as a p35 inhibitor, exhibits remarkable selectivity in binding to cyclin-dependent kinases through a combination of steric hindrance and hydrogen bonding. Its structural features promote a unique orientation that stabilizes the enzyme-inhibitor complex, effectively modulating kinase activity. The compound's kinetic profile reveals a slow dissociation rate, allowing for sustained interaction with target proteins, thereby influencing downstream signaling mechanisms.

A specific inhibitor of CDK7/9, which also inhibits CDK5 at higher concentrations.