KIR2.1 Inhibitors

Baicalein, a flavonoid found in Scutellaria baicalensis, inhibits KIR2.1 by modulating the Akt/mTOR signaling pathway. Baicalein suppresses Akt activation, leading to the inhibition of mTOR, a downstream effector involved in KIR2.1 regulation. The disruption of this pathway results in reduced expression and activity of KIR2.1, providing a mechanistic insight into how baicalein acts as a direct inhibitor of KIR2.1 by targeting the Akt/mTOR signaling axis.

ML133, a small molecule, acts as a KIR2.1 inhibitor by targeting its ion channel. This compound binds to the channel pore, impeding ion flux through KIR2.1. ML133′s direct interaction with the ion channel region of KIR2.1 elucidates its inhibitory mechanism, providing a molecular basis for its potential as a pharmacological inhibitor of KIR2.1 function.

Clofilium, a class III antiarrhythmic agent, inhibits KIR2.1 by modulating the channel's kinetics. It slows the activation and deactivation kinetics of KIR2.1, resulting in decreased ion conductance. The modulation of channel kinetics by clofilium illustrates its direct inhibitory impact on KIR2.1, revealing a pharmacological approach to regulate the activity of this potassium channel.

Paxilline, a mycotoxin found in Penicillium paxilli, inhibits KIR2.1 by selectively blocking the channel pore. This compound interferes with ion permeation through KIR2.1, disrupting its normal physiological function. Paxilline′s specific interaction with the channel pore underscores its direct inhibitory role in modulating KIR2.1, providing insights into the potential use of mycotoxin-derived compounds as targeted inhibitors of ion channel activity.

Glibenclamide, an ATP-sensitive potassium (KATP) channel inhibitor, indirectly influences KIR2.1 by blocking KATP channels. Inhibition of KATP channels depolarizes the cell membrane, altering the electrochemical gradient across the membrane and indirectly affecting KIR2.1 activity

Barium chloride inhibits KIR2.1 by directly blocking the channel pore. This compound hinders ion permeation through the channel, disrupting its normal function. Barium chloride′s specific interaction with the channel pore underscores its direct inhibitory role in modulating KIR2.1, providing insights into the potential use of metal ions as direct inhibitors of ion channel activity.

Nifedipine, a calcium channel blocker, indirectly inhibits KIR2.1 by modulating intracellular calcium levels. By blocking calcium channels, nifedipine reduces intracellular calcium concentrations, indirectly influencing KIR2.1 activity. The indirect inhibition of KIR2.1 by nifedipine highlights the intricate crosstalk between calcium signaling and potassium channel regulation, offering a pharmacological approach to modulate KIR2.1 function through calcium channel interference.

4-Aminopyridine inhibits KIR2.1 by blocking delayed rectifier potassium channels. This compound disrupts potassium currents, affecting the electrochemical balance necessary for KIR2.1 function. The indirect inhibition of KIR2.1 by 4-aminopyridine illustrates the interconnectedness of potassium channels and offers a pharmacological avenue for modulating KIR2.1 activity through delayed rectifier potassium channel interference.

Linopirdine, a selective blocker of voltage-gated potassium channels, indirectly inhibits KIR2.1 by targeting other potassium channels. By blocking specific potassium channels, linopirdine alters the electrochemical balance, indirectly influencing KIR2.1 activity. T

XE991, a blocker of KCNQ potassium channels, indirectly inhibits KIR2.1 by targeting other potassium channels. By blocking KCNQ channels, XE991 disrupts potassium currents, affecting the electrochemical balance necessary for KIR2.1 function. The indirect inhibition of KIR2.1 by XE991 illustrates the intricate crosstalk between different potassium channels and offers a pharmacological avenue for modulating KIR2.1 activity through selective potassium channel interference.