Apamin, an 18 amino acid peptide neurotoxin found in apitoxin (bee venom), is known to block Ca2+-activated K+ channels and prevent carbon tetrachloride-induced liver fibrosis.
CAT No: R1209
CAS No:24345-16-2
Synonyms/Alias:Apamin;24345-16-2;UNII-X644P85KUR;EINECS 246-182-7;Ro 23-6721;Apamine;X644P85KUR;DTXSID70897227;Apamin (reduced) cyclic (1-11),(3-15)-bis(disulfide);L-Histidinamide, L-cysteinyl-L-asparaginyl-L-cysteinyl-L-lysyl-L-alanyl-L-prolyl-L-alpha-glutamyl-L-threonyl-L-alanyl-L-leucyl-L-cysteinyl-L-alanyl-L-arginyl-L-arginyl-L-cysteinyl-L-glutaminyl-L-glutaminyl-, cyclic (1-11)(3-15)-bis(disulfide);C79H131N31O24S4;APAMIN [MI];DTXCID201326617;HB1051;MFCD00167944;AKOS024456726;FA73204;DA-50626;Apamin, Bee Venom - CAS 24345-16-2;NS00075519;RO-23-6721;G12450;Q417260;APAMIN (REDUCED), CYCLIC (1->11),(3->15)-BIS(DISULFIDE);246-182-7;L-HISTIDINAMIDE, L-CYSTEINYL-L-ASPARAGINYL-L-CYSTEINYL-L-LYSYL-L-ALANYL-L-PROLYL-L-.ALPHA.-GLUTAMYL-L-THREONYL-L-ALANYL-L-LEUCYL-L-CYSTEINYL-L-ALANYL-L-ARGINYL-L-ARGINYL-L-CYSTEINYL-L-GLUTAMINYL-L-GLUTAMINYL-, CYCLIC (1->11),(3->15)-BIS(DISULFIDE);L-HISTIDINAMIDE, L-CYSTEINYL-L-ASPARAGINYL-L-CYSTEINYL-L-LYSYL-L-ALANYL-L-PROLYL-L-ALPHA-GLUTAMYL-L-THREONYL-L-ALANYL-L-LEUCYL-L-CYSTEINYL-L-ALANYL-L-ARGINYL-L-ARGINYL-L-CYSTEINYL-L-GLUTAMINYL-L-GLUTAMINYL-, CYCLIC (1->11),(3->15)-BIS(DISULFIDE);
Apamin is a peptide neurotoxin isolated from the venom of the honeybee (Apis mellifera), notable for its unique ability to selectively block small-conductance calcium-activated potassium (SK) channels. As a naturally occurring polypeptide comprising 18 amino acids, apamin has become a valuable research tool in neurophysiology and ion channel pharmacology. Its high specificity for SK channels has positioned it as a critical molecular probe for investigating neuronal excitability, synaptic plasticity, and the functional roles of potassium channels in various biological systems. By enabling precise modulation of SK channel activity, apamin supports advanced studies into the complex mechanisms underlying neural signaling and cellular communication.
Electrophysiological research: Apamin is widely utilized in electrophysiological studies to characterize the properties and physiological functions of SK channels in neurons and other excitable cells. Its ability to selectively inhibit these channels allows researchers to dissect the contributions of SK-mediated potassium currents to membrane potential regulation, action potential firing patterns, and afterhyperpolarization phenomena. By applying this peptide in patch-clamp or other electrophysiological assays, scientists can elucidate the role of SK channels in shaping neuronal output and synaptic integration, providing critical insights into the fundamental principles of cellular excitability.
Neuropharmacology and signal transduction studies: The selective action of apamin on SK channels makes it an essential tool for neuropharmacological investigations into signal transduction pathways. Researchers leverage its specificity to explore the downstream effects of SK channel modulation on neurotransmitter release, synaptic plasticity, and intracellular calcium dynamics. By employing apamin in combination with other channel modulators or signaling pathway inhibitors, studies can precisely map the molecular cascades that regulate neuronal communication, synaptic strength, and plastic changes associated with learning and memory.
Ion channel screening and drug discovery: Apamin serves as a reference compound in high-throughput screening assays and drug discovery programs aimed at identifying novel modulators of SK channels. Its well-characterized pharmacological profile provides a benchmark for evaluating the potency, selectivity, and mechanism of action of new synthetic or natural compounds targeting the same channel family. By incorporating apamin into assay development and validation workflows, researchers can ensure the reliability and specificity of their screening platforms, facilitating the discovery of innovative agents for research and potential therapeutic applications in the context of ion channelopathies.
Neurotoxin structure-function analysis: As a prototypical peptide neurotoxin, apamin is frequently employed in structural biology and mutagenesis studies to investigate the relationship between peptide conformation and channel-blocking activity. By examining the effects of specific amino acid substitutions or modifications on its interaction with SK channels, researchers can unravel the molecular determinants of selectivity and binding affinity. These structure-function analyses not only deepen understanding of toxin-channel interactions but also inform the rational design of novel peptide-based modulators with tailored selectivity profiles for research use.
Comparative physiology and evolutionary biology: Apamin is also applied in comparative studies to assess the conservation and divergence of SK channel function across species and tissue types. By analyzing the effects of this peptide in diverse biological systems, researchers can probe the evolutionary adaptations of potassium channel families and their contributions to organismal physiology. Such investigations expand knowledge of how ion channel diversity shapes neural circuitry and adaptive responses, offering broader perspectives on the molecular evolution of nervous systems.
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