Overview
- Rupasinghe, D.B. et al. (2020) Biochem. Pharmacol., 181, 114080.
Alomone Labs Pe1b inhibits NaV1.7 channel currents heterologously expressed in Xenopus oocytes.A. Representative time course of Pe1b (#STP-050) inhibition of NaV1.7 channels current. Membrane potential was held at -100 mV, current was elicited by a 100 ms voltage step to 0 mV every 10 sec, and significantly inhibited by application of 50 nM (magenta) and 500 nM (green) Pe1b.
B. Superimposed traces of NaV1.7 channel currents in the absence (control) and presence of 50 nM (magenta) and 500 nM (green) Pe1b (taken from the recording in A).
- Rupasinghe, D.B. et al. (2020) Biochem. Pharmacol., 181, 114080.
- Klint, J.K. et al. (2012) Toxicon, 60, 478.
β/μ-theraphotoxin-Pe1b (Pe1b) is a 34 amino acid peptidyl toxin isolated from the venom of the arboreal tarantula Phormingochilus everetti1. Pe1b is a voltage-gated sodium (Nav) channel inhibitor, and it has the greatest inhibitory activity against Nav1.7. Pe1b contains three disulfide bonds that form an inhibitory cysteine-knot (ICK) architectural motif. Its ICK motif belonging to the Nav-targeting spider toxin (NaSpTx) family 2, which contains the most members amongst the 12 sodium channel toxin families (NaSpTx1- NaSpTx12)1,2.
Pe1b is highly similar to Protoxin-1 (ProTx-I), which is also an inhibitor of Nav1.7. The C-terminus of both toxins interact with Nav1.71.
Nav channels are involved in a wide array of physiological processes. In particular, Nav1.7 plays a critical role in the generation and conduction of action potentials. It is also active in pain sensing nerves. Thus, Pe1b may be an important tool for the study of pain, pain treatment, and the development of analgesics.
Pe1b (#STP-050) is a highly pure, synthetic, and biologically active peptide toxin.
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