330 € – 1155 €
ω-Hexatoxin-Hv1a (ω-HXTX-Hv1a, ω-atracotoxin-Hv1a, ω-ACTX-Hv1a) has been isolated from the venom of Australian funnel web spiders. ω-Hexatoxin-Hv1a has been described to block mid-low- (M-LVA) and high-voltage-activated (HVA) insect calcium channel (Ca(v)) currents.
AA sequence: SPTCIPSGQPCPYNENCCSQSCTFKENENGNTVKRCD
Disulfide bonds: Cys4-Cys18; Cys11-Cys22; Cys17-Cys36
Length (aa): 37
Formula: C162H247N49O61S6
Molecular Weight: 4049.42 g/mol
CAS number: NA
Source: Synthetic
Purity rate: > 95 %
Fletcher J., et al. (1997) The structure of a novel insecticidal neurotoxin, omega-atracotoxin-HV1, from the venom of an Australian funnel web spider. Nat Struct Biol. PMID: 9228949
A family of potent insecticidal toxins has recently been isolated from the venom of Australian funnel web spiders. Among these is the 37-residue peptide omega-atracotoxin-HV1 (omega-ACTX-HV1) from Hadronyche versuta. We have chemically synthesized and folded omega-ACTX-HV1, shown that it is neurotoxic, ascertained its disulphide bonding pattern, and determined its three-dimensional solution structure using NMR spectroscopy. The structure consists of a solvent-accessible beta-hairpin protruding from a disulphide-bonded globular core comprising four beta-turns. The three intramolecular disulphide bonds from a cystine knot motif similar to that seen in several other neurotoxic peptides. Despite limited sequence identity, omega-ACTX-HV1 displays significant structural homology with the omega-agatoxins and omega-conotoxins, both of which are vertebrate calcium channel antagonists; however, in contrast with these toxins, we show that omega-ACTX-HV1 inhibits insect, but not mammalian, voltage-gated calcium channel currents.
