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Other names U1-agatoxin-Aop1a, U1-AGTX-Aop1a | |
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Molar mass | 3500 g/mol |
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). |
Agelenin (toxicologically named as U1-agatoxin-Aop1a [1] and abbreviated as U1-AGTX-Aop1a) is a neurotoxic peptide isolated from the venom of the spider Allagelena opulenta which consists of 35 amino acids. It is an antagonist of the presynaptic P-type calcium channel in insects.
Agelenin is an insecticidal toxin of the venom of the species Allagelena opulenta . [1] It was first discovered in 1990. [2]
Agelenin consists of a polypeptide chain of 35 amino acid residues. [2] It has a short anti-parallel β-sheet connected by three disulfide bonds and four β-turns that form the compact core structure. The three amino acid residues that are thought to be essential for the inhibiting activity of agelenin are Phe9, Ser28 and Arg33. [3]
The structure of agelenin is similar to the structure of ICK toxins like ω-Aga-IVA and ω-ACTXHv1a in that they all consist of three disulfide bonds with the same bonding pattern. An important difference between agelenin and ω-Aga-IVA and ω-ACTXHv1a is that ω-Aga-IVA and ω-ACTXHv1a have functional C-terminal tails. [3]
Agelenin belongs to toxin group of agatoxins. [1] The amino acid structure of agelenin is Gly-Gly-Cys-Leu-Pro-His-Asn-Arg-Phe-Cys-Asn-Ala-Leu-Ser-Gly-Pro-Arg-Cys-Cys-Ser-Gly-Leu-Lys-Cys-Lys-Glu-Leu-Ser-Ile-Trp-Asp-Ser-Arg-Cys-Leu (GGCLPHNRFCNALSGPRCCSGLKCKELSIWDSRCL). [3]
Agelenin is directed against P-subtype calcium channels in insects. [4]
Agelenin is not toxic in mammals, but has a PD50 of 291 pmol/g in crickets where it causes rapid, reversible paralysis. [3] In preparations of neuromuscular junctions of lobsters agelenin causes a non-reversible paralysis due to the suppression of excitatory postsynaptic potentials, presumably by inhibition of the presynaptic calcium influx. [2]
Ziconotide, sold under the brand name Prialt, also called intrathecal ziconotide (ITZ) because of its administration route, is an atypical analgesic agent for the amelioration of severe and chronic pain. Derived from Conus magus, a cone snail, it is the synthetic form of an ω-conotoxin peptide. It is 1,000 times as powerful as morphine.
Neurophysin I is a carrier protein with a size of 10 KDa and contains 90 to 97 amino acids. It is a cleavage product of preprooxyphysin. It is a neurohypophysial hormone that is transported in vesicles with oxytocin, the other cleavage product, along axons, from magnocellular neurons of the hypothalamus to the posterior lobe of the pituitary. Although it is stored in neurosecretory granules with oxytocin and released with oxytocin, its biological action is unclear.
omega-Grammotoxin SIA (ω-grammotoxin SIA) is a protein toxin that inhibits P, Q, and N voltage-gated calcium channels (Ca2+ channels) in neurons.
Agitoxin is a toxin found in the venom of the scorpion Leiurus quinquestriatus hebraeus. Other toxins found in this species include charybdotoxin (CTX). CTX is a close homologue of Agitoxin.
Grammotoxin is a toxin in the venom of the tarantula Grammostola spatulata. It is a protein toxin that inhibits P-, Q- and N-type voltage-gated calcium channels in neurons. Grammotoxin is also known as omega-grammotoxin SIA.
Neurophysin II is a carrier protein with a size of 19,687.3 Da and is made up of a dimer of two virtually identical chains of amino acids. Neurophysin II is a cleavage product of the AVP gene. It is a neurohypophysial hormone that is transported in vesicles with vasopressin, the other cleavage product, along axons, from magnocellular neurons of the hypothalamus to the posterior lobe of the pituitary. Although it is stored in neurosecretory granules with vasopressin and released with vasopressin into the bloodstream, its biological action is unclear. Neurophysin II is also known as a stimulator of prolactin secretion.
Agatoxins are a class of chemically diverse polyamine and peptide toxins which are isolated from the venom of various spiders. Their mechanism of action includes blockade of glutamate-gated ion channels, voltage-gated sodium channels, or voltage-dependent calcium channels. Agatoxin is named after the funnel web spider which produces a venom containing several agatoxins. There are different agatoxins. The ω-agatoxins are approximately 100 amino acids in length and are antagonists of voltage-sensitive calcium channels and also block the release of neurotransmitters. For instance, the ω-agatoxin 1A is a selective blocker and will block L-type calcium channels whereas the ω-agatoxin 4B will inhibit voltage sensitive P-type calcium channels. The μ-agatoxins only act on insect voltage-gated sodium channels.
Pompilidotoxins (PMTXs) are toxic substances that can only be found in the venom of several solitary wasps. This kind of wasp uses their venom to offensively capture prey and is relatively harmless to humans. This is in stark contrast to social insects that defend themselves and their colonies with their venom.
BeKm-1 is a toxin from the Central Asian scorpion Buthus eupeus. BeKm-1 acts by selectively inhibiting the human Ether-à-go-go Related Gene (hERG) channels, which are voltage gated potassium ion channels.
Helothermine is a toxin from the venom of the Mexican beaded lizard Heloderma horridum horridum. Helothermine inhibits ryanodine receptors, calcium channels and potassium channels. Helothermine can cause lethargy, partial paralysis of rear limbs and lowering of the body temperature.
delta-Palutoxins (δ-palutoxins) consist of a homologous group of four insect-specific toxins from the venom of the spider Pireneitega luctuosa. They show a high toxicity against Spodoptera litura larvae by inhibiting sodium channels, leading to strong paralytic activity and eventually to the death of the insect.
Guangxitoxin, also known as GxTX, is a peptide toxin found in the venom of the tarantula Plesiophrictus guangxiensis. It primarily inhibits outward voltage-gated Kv2.1 potassium channel currents, which are prominently expressed in pancreatic β-cells, thus increasing insulin secretion.
Hanatoxin is a toxin found in the venom of the Grammostola spatulata tarantula. The toxin is mostly known for inhibiting the activation of voltage-gated potassium channels, most specifically Kv4.2 and Kv2.1, by raising its activation threshold.
Huwentoxins (HWTX) are a group of neurotoxic peptides found in the venom of the Chinese bird spider Haplopelma schmidti. The species was formerly known as Haplopelma huwenum, Ornithoctonus huwena and Selenocosmia huwena. While structural similarity can be found among several of these toxins, HWTX as a group possess high functional diversity.
CgNa is a peptide toxin isolated from the sea anemone Condylactis gigantea. It causes an increased action potential duration by slowing down the inactivation of tetrodotoxin-sensitive sodium channels.
Centruroides suffusus suffusus toxin II (CssII) is a scorpion β-toxin from the venom of the scorpion Centruroides suffusus suffusus. CssII primarily affects voltage-gated sodium channels by causing a hyperpolarizing shift of voltage dependence, a reduction in peak transient current, and the occurrence of resurgent currents.
Vejocalcin (VjCa, also called Vejocalcine) is a toxin from the venom of the Mexican scorpion Vaejovis mexicanus. Vejocalcin is a member of the calcin family of toxins. It acts as a cell-penetrating peptide (CPP); it binds with high affinity and specificity to skeletal ryanodine receptor 1 (RYR1) of the sarcoplasmic reticulum, thereby triggering calcium release from intracellular Ca2+ stores.
LmαTX5 is an α-scorpion toxin which inhibits the fast inactivation of voltage-gated sodium channels. It has been identified through transcriptome analysis of the venom gland of Lychas mucronatus, also known as the Chinese swimming scorpion – a scorpion species which is widely distributed in Southeast Asia.
DKK-SP1 is one of the many neurotoxins present in the scorpion Mesobuthus martensii. This toxin inhibits the voltage-gated sodium channel Nav1.8.
Protoxin-I, also known as ProTx-I, or Beta/omega-theraphotoxin-Tp1a, is a 35-amino-acid peptide neurotoxin extracted from the venom of the tarantula Thrixopelma pruriens. Protoxin-I belongs to the inhibitory cystine knot (ICK) family of peptide toxins, which have been known to potently inhibit voltage-gated ion channels. Protoxin-I selectively blocks low voltage threshold T-type calcium channels, voltage gated sodium channels and the nociceptor cation channel TRPA1. Due to its unique ability to bind to TRPA1, Protoxin-I has been implicated as a valuable pharmacological reagent with potential applications in clinical contexts with regards to pain and inflammation
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