Structure via PubChem · Public domain (PubChem)
apamin
Sign in to saveApamin is an 18 amino acid globular peptide neurotoxin found in apitoxin (bee venom). Dry bee venom consists of 2–3% of apamin. Apamin selectively blocks SK channels, a type of Ca2+-activated K+ channel expressed in the central nervous system. Toxicity is caused by only a few amino acids, in particular cysteine1, lysine4, arginine13, arginine14 and histidine18. These amino acids are involved in the binding of apamin to the Ca2+-activated K+ channel. Due to its specificity for SK channels, apamin is used as a drug in biomedical research to study the electrical properties of SK channels and thei
In the Vinony graph
Within Vinony's link graph, apamin is referenced by 110 other articles, and connects out to amino acid, peptide and Guillain–Barré syndrome.
It is catalogued under topics including Chembox image size set, Cyclic peptides and ECHA InfoCard ID from Wikidata.
Its subject is documented across 13 Wikipedia language editions.
Key facts
- Protein.Name
- Apamin Preproprotein
- Protein.Symbol
- Apamin
- Protein.CAS_number
- 24345-16-2
- Protein.EntrezGene
- 406135
- Protein.UniProt
- P01500
via Wikipedia infobox
Chemical data
- Formula
- C79H131N31O24S4
- Molecular weight
- 2027.4 g/mol
- IUPAC name
- 3-[(1R,4S,7S,13S,16S,19S,22S,25S,28R,31S,34S,37S,40R,47S,50R)-50-amino-40-[[(2S)-5-amino-1-[[(2S)-5-amino-1-[[(2S)-1-amino-3-(1H-imidazol-4-yl)-1-oxopropan-2-yl]amino]-1,5-dioxopentan-2-yl]amino]-1,5-dioxopentan-2-yl]carbamoyl]-4-(4-aminobutyl)-47-(2-amino-2-oxoethyl)-34,37-bis(3-carbamimidamidopropyl)-19-[(1R)-1-hydroxyethyl]-7,22,31-trimethyl-25-(2-methylpropyl)-2,5,8,14,17,20,23,26,29,32,35,38,46,49-tetradecaoxo-42,43,52,53-tetrathia-3,6,9,15,18,21,24,27,30,33,36,39,45,48-tetradecazatricyclo[26.16.10.09,13]tetrapentacontan-16-yl]propanoic acid
- SMILES
- C[C@H]1C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](CSSC[C@H]2C(=O)N[C@H](C(=O)N[C@H](C(=O)N3CCC[C@H]3C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](CSSC[C@@H](C(=O)N[C@H](C(=O)N2)CC(=O)N)N)C(=O)N1)CC(C)C)C)[C@@H](C)O)CCC(=O)O)C)CCCCN)C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CC4=CNC=N4)C(=O)N)CCCNC(=N)N)CCCNC(=N)N
- InChIKey
- YVIIHEKJCKCXOB-STYWVVQQSA-N
- XLogP
- -13.4
- Polar surface area
- 1020 Ų
- H-bond donors
- 31
- H-bond acceptors
- 33
- Formal charge
- 0
via PubChem
Drug data · ChEMBL
- Molecule type
- Protein
via ChEMBL · EBI
Research
3,407 papers- Apamin.Pharmacology & therapeutics · 1984
- Therapeutic Effects of Apamin as a Bee Venom Component for Non-Neoplastic Disease.Toxins · 2020
- Apamin Improves Prefrontal Nicotinic Impairment in Mouse Model of Alzheimer's Disease.Cerebral cortex (New York, N.Y. : 1991) · 2020
- Apamin Enhances Neurite Outgrowth and Regeneration after Laceration Injury in Cortical Neurons.Toxins · 2021
- The therapeutic potential of bee venom-derived Apamin and Melittin conjugates in cancer treatment: A systematic review.Pharmacological research · 2024
via PubMed
Wikidata facts
Show 4 more facts
- chemical formula
- C₇₉H₁₃₁N₃₁O₂₄S₄
- isomeric SMILES
- C[C@H]1C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](CSSC[C@H]2C(=O)N[C@H](C(=O)N[C@H](C(=O)N3CCC[C@H]3C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](CSSC[C@@H](C(=O)N[C@H](C(=O)N2)CC(=O)N)N)C(=O)N1)CC(C)C)C)[C@@H](C)O)CCC(=O)O)C)CCCCN)C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CC4=CNC=N4)C(=O)N)CCCNC(=N)N)CCCNC(=N)N
- canonical SMILES
- CC1C(=O)NC(C(=O)NC(C(=O)NC(CSSCC2C(=O)NC(C(=O)NC(C(=O)N3CCCC3C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(CSSCC(C(=O)NC(C(=O)N2)CC(=O)N)N)C(=O)N1)CC(C)C)C)C(C)O)CCC(=O)O)C)CCCCN)C(=O)NC(CCC(=O)N)C(=O)NC(CCC(=O)N)C(=O)NC(CC4=CNC=N4)C(=O)N)CCCNC(=N)N)CCCNC(=N)N
- subject has role
- neurotoxin
Sources (2)
via Wikidata · CC0
~10 min read
Encyclopedic overview
9 sectionsContents
- Origin
- Structure and active site
- Toxicodynamics
- Toxicokinetics
- Symptoms
- Toxicity rates
- Therapeutic use
- References
- External links
Apamin is an 18 amino acid globular peptide neurotoxin found in apitoxin (bee venom). Dry bee venom consists of 2–3% of apamin. Apamin selectively blocks SK channels, a type of Ca2+-activated K+ channel expressed in the central nervous system. Toxicity is caused by only a few amino acids, in particular cysteine1, lysine4, arginine13, arginine14 and histidine18. These amino acids are involved in the binding of apamin to the Ca2+-activated K+ channel. Due to its specificity for SK channels, apamin is used as a drug in biomedical research to study the electrical properties of SK channels and their role in the afterhyperpolarizations occurring immediately following an action potential.
==Origin== The first symptoms of apitoxin (bee venom), that are now thought to be caused by apamin, were described back in 1936 by Hahn and Leditschke. Apamin was first isolated by Habermann in 1965 from Apis mellifera, the Western honey bee. Apamin was named after this bee. Bee venom contains many other compounds, like histamine, phospholipase A2, hyaluronidase, MCD peptide, and the main active component melittin. Apamin was separated from the other compounds by gel filtration and ion exchange chromatography.
Excerpted from Wikipedia’s “apamin” article, available under the CC BY-SA 4.0 licence.