Rsk-1 Inhibitors

Ro 31-8220 is a selective inhibitor of Rsk-1, a serine/threonine kinase involved in various signaling pathways. It disrupts the phosphorylation of target substrates, thereby modulating downstream effects on cell growth and survival. The compound exhibits unique binding interactions that stabilize the inactive conformation of Rsk-1, influencing its catalytic activity. Its kinetic profile reveals a competitive inhibition mechanism, highlighting its specificity and potency in disrupting kinase-mediated signaling cascades.

Fasudil, Monohydrochloride Salt acts as a potent inhibitor of Rsk-1, engaging in specific molecular interactions that alter the enzyme's conformation. This compound exhibits a unique ability to interfere with the ATP-binding site, effectively hindering the phosphorylation process. Its reaction kinetics suggest a non-competitive inhibition model, allowing for a nuanced modulation of kinase activity. The compound's solubility and stability in various environments further enhance its interaction dynamics within cellular pathways.

Ageladine A, TFA selectively targets Rsk-1 through a unique binding mechanism that stabilizes an inactive conformation of the kinase. This compound exhibits a distinct affinity for the enzyme's regulatory domain, disrupting its interaction with upstream signaling molecules. The kinetics of Ageladine A reveal a mixed inhibition pattern, allowing for both competitive and non-competitive effects on substrate phosphorylation. Its robust solubility profile facilitates effective cellular uptake, enhancing its modulatory potential in signaling cascades.

A synthetic compound targeting RSK-1 and RSK-2 by binding to their N-terminal kinase domain.

BI-D1870 is a selective inhibitor of Rsk-1 that operates through a unique allosteric modulation mechanism, altering the enzyme's conformational dynamics. This compound preferentially binds to the kinase's active site, preventing substrate access and effectively blocking phosphorylation events. Its interaction with the enzyme is characterized by a rapid association and slower dissociation, indicating a high affinity. Additionally, BI-D1870 demonstrates favorable physicochemical properties, enhancing its stability in various environments.

BRD 7389 is a potent inhibitor of Rsk-1, distinguished by its ability to disrupt the enzyme's catalytic activity through competitive binding at the ATP site. This compound exhibits a unique kinetic profile, with a fast on-rate and a prolonged off-rate, suggesting a strong interaction with the enzyme. Its structural features facilitate specific hydrogen bonding and hydrophobic interactions, enhancing selectivity. Furthermore, BRD 7389's solubility characteristics allow for effective engagement in diverse biochemical assays.

Originally a PKCβ inhibitor, it also inhibits RSK-1 among other kinases.

Known as an mTOR inhibitor, it has also been reported to inhibit RSK-1 and RSK-2.

A reversible and ATP-competitive inhibitor of RSK-1 and RSK-2, used in research.