IKK beta Inhibitors

IKK-2 Inhibitor IV is a selective inhibitor of IKKβ. It acts by competing with ATP for the ATP-binding site in the kinase domain, thereby preventing the phosphorylation of IκBα and the subsequent activation of NF-κB.

Piceatannol functions as an IKK beta inhibitor, engaging in specific molecular interactions that modulate the NF-kB signaling pathway. It exhibits a unique binding affinity that alters the enzyme's conformation, effectively hindering its activity. The compound's distinct reaction kinetics suggest a competitive inhibition mechanism, influencing downstream signaling events. Its structural characteristics facilitate targeted disruption of inflammatory responses, showcasing its role in cellular regulation.

Wedelolactone is a naturally occurring IKK inhibitor. It inhibits IKK by directly binding to the ATP binding site in the kinase domain, thereby preventing the phosphorylation and degradation of IκB proteins, and hence inhibiting NF-κB activation.

SC-514 is an IKKβ inhibitor. It binds to the ATP-binding pocket of IKKβ, thus inhibiting the phosphorylation and degradation of IκBα, which subsequently inhibits the activation of NF-κB.

Aspirin acts as an IKK beta inhibitor by forming hydrogen bonds with key amino acid residues, leading to a conformational change that reduces enzyme activity. Its unique structural features allow for selective interaction with the IKK complex, influencing the phosphorylation of downstream targets. The compound exhibits a non-competitive inhibition profile, impacting the kinetics of the NF-kB pathway. This modulation highlights its potential in regulating cellular stress responses and inflammatory processes.

BMS-345541 is a highly selective inhibitor of IKK. It binds to an allosteric site of IKKβ, interrupting the phosphorylation and subsequent degradation of IκBα, thereby blocking NF-κB activation.

IKK-16 is an IKKβ inhibitor. It works by binding to the ATP-binding site of IKKβ, inhibiting the kinase activity and preventing the phosphorylation and degradation of IκBα, thereby blocking NF-κB activation.

NFκB Activation Inhibitor VI, BOT-64, selectively targets IKK beta through specific hydrophobic interactions and electrostatic forces, stabilizing a less active enzyme conformation. This compound disrupts the phosphorylation cascade within the NF-kB signaling pathway, altering reaction kinetics and downstream signaling dynamics. Its unique molecular architecture facilitates precise binding, influencing cellular responses to stress and modulating inflammatory signaling pathways effectively.

CAY10657 is a selective inhibitor of IKK beta, characterized by its unique ability to engage in specific hydrogen bonding and hydrophobic interactions with the enzyme's active site. This compound effectively alters the conformational dynamics of IKK beta, leading to a reduction in its kinase activity. By modulating the phosphorylation events within the NF-kB pathway, CAY10657 influences cellular signaling cascades, thereby impacting various cellular processes and responses to stimuli.

ML120B is a selective inhibitor of IKKβ. It works by blocking the kinase activity of IKKβ, leading to the inhibition of IκBα phosphorylation and degradation, and thus blocking NF-κB activation.