Tertiapin

Tertiapin is a potent and selective inhibitor of the inward-rectifier potassium channels (Kir), specifically Kir1.1 and Kir3.x. It is a peptide that was originally isolated from the venom of the honey bee Apis mellifera.

Structure

Tertiapin consists of 21 amino acid residues and has a molecular weight of approximately 2.5 kDa. The peptide has a compact structure stabilized by two disulfide bridges.

Function

Tertiapin blocks the Kir1.1 and Kir3.x channels by binding to the pore region of the channel, thereby preventing the flow of potassium ions through the channel. This blockage can affect various physiological processes, including heart rate, insulin secretion, and neuronal excitability.

Clinical significance

Due to its ability to selectively inhibit certain Kir channels, tertiapin has potential therapeutic applications. For example, it could be used to treat diseases associated with abnormal Kir channel activity, such as certain types of cardiac arrhythmias, diabetes, and epilepsy.

See also

• Inward-rectifier potassium ion channels
• Venom
• Peptide

References

Tertiapin Resources
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