Tertiapin Q is a stable derivative of the bee venom toxin tertiapin. It is a high affinity blocker for inward-rectifier K+ channels that binds to ROMK1 (Kir1.1) and GIRK1/4 (Kir3.1/3.4) channels with high affinity (Ki values are 1.3 and 13.3 nM respectively).
CAT No: R1101
CAS No:910044-56-3
Synonyms/Alias:910044-56-3;TPN(Q);AKOS024456523;
Tertiapin-Q is a synthetic peptide derivative originally based on a natural peptide isolated from honey bee venom, engineered for enhanced stability and selectivity. As a 21-amino acid peptide, it is distinguished by its ability to modulate specific ion channels, particularly inward-rectifier potassium (Kir) channels, including Kir1.1 and Kir3.x subtypes. Its highly selective binding properties and resistance to proteolytic degradation have established it as a valuable molecular tool in electrophysiological, neurobiological, and cardiovascular research. The unique sequence modifications in Tertiapin-Q confer improved experimental utility, making it a preferred choice for dissecting potassium channel function and signaling pathways in various biological systems.
Ion Channel Characterization: Tertiapin-Q is widely employed in the functional analysis of Kir channels, especially in patch-clamp and other electrophysiological studies. By selectively inhibiting Kir1.1 and Kir3.x channels, the peptide enables researchers to isolate and define the contributions of these channels to membrane potential regulation and cellular excitability. Its high specificity allows for precise mapping of channel function in neuronal, cardiac, and renal cell types, supporting the elucidation of ion channel physiology and pathophysiology in controlled experimental settings.
Neuropharmacology Research: In neurobiology, Tertiapin-Q serves as a potent tool to investigate the role of G-protein-gated inwardly rectifying potassium (GIRK) channels in synaptic transmission and neuronal signaling. Its application helps clarify the involvement of GIRK channels in modulating neurotransmitter release, neuronal firing patterns, and overall network activity. This targeted inhibition has proven essential for studies aiming to unravel the molecular mechanisms underlying synaptic plasticity, neural circuit modulation, and the interplay between ion channel activity and neurotransmission.
Cardiac Electrophysiology: The peptide is instrumental in cardiac research, where its selective blockade of Kir channels facilitates the study of cardiac action potential dynamics and arrhythmogenesis. By inhibiting specific potassium currents, Tertiapin-Q enables detailed investigation of their roles in cardiac repolarization, rhythm stability, and susceptibility to arrhythmic events. This application supports the development of mechanistic models of cardiac electrophysiology and provides a platform for testing hypotheses related to ion channel dysfunction in cardiac tissues.
Renal Physiology Studies: Tertiapin-Q is also utilized in the examination of renal potassium handling and electrolyte transport. Its activity against Kir1.1 channels, which are expressed in the distal nephron, allows researchers to probe the molecular mechanisms governing potassium secretion and reabsorption. Through selective channel inhibition, the peptide supports studies into the regulation of renal electrolyte balance, contributing to a deeper understanding of kidney function at the cellular and systemic levels.
Peptide Pharmacology and Structure-Activity Relationship Analysis: As a chemically modified peptide, Tertiapin-Q is valuable for exploring the structure-activity relationships of peptide-channel interactions. Its use in comparative studies with other peptide analogs or channel blockers provides insight into the critical determinants of selectivity, affinity, and stability. This application aids in guiding the rational design of next-generation peptide modulators and informs the development of novel experimental probes for ion channel research.
The stability of TPNQ allows us to investigate how it interacts with the targeted channels. We found that the interaction between TPNQ and the ROMK1 channel is a bimolecular reaction, i.e., one TPNQ molecule binds to one channel. The interaction surface in TPNQ is primarily formed by its α helix rather than the β sheets with which scorpion toxins form their interaction surface. The mutagenesis studies on both the channel and TPNQ together strongly suggest that to block the K+pore TPNQ plugs its α helix into the vestibule of the K+ pore, while leaving the extended structural portion sticking out of the vestibule into the extracellular media.
Mechanisms of Inward-Rectifier K+ Channel Inhibition by Tertiapin-Q
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