Overview
- Chow, C.Y. et al. (2015) Toxins 7, 2494.
Alomone Labs Phlo1b inhibits NaV1.7 channels expressed in Xenopus oocytes.A. Time course of Phlo1b (#STP-370) inhibition of NaV1.7 channel currents. Membrane potential was held at -100 mV, current was elicited by a 100 ms voltage step to -10 mV delivered every 10 sec, and was significantly inhibited by a 3 min application of 200 nM Phlo1b (green bar). B. Superimposed traces of NaV1.7 channel currents upon application of control (black) and of 200 nM Phlo1b (green), taken from the recording shown in A.
- Chow, C.Y. et al. (2015) Toxins 7, 2494.
- Klint J.K. et al. (2015) Br. J. Pharmacol. 172, 2445.
Phlo1b is a NaV1.7 channels blocker, originally isolated from the venom of the Australian Phlogius sp. Tarantula. The peptide toxin is a gating modifier that inhibits NaV1.7 activation through its interaction with one or more voltage-sensor domains and displays an IC50 value of 0.36 µM1.
Phlo1b is a 35-residue peptide that belongs to the NaSpTx2 family and is a valuable research tool and lead molecule for the development of ion channel therapeutics. NaSpTx2 family peptides contain three disulfide bonds and they share highly stable inhibitor cystine knot (ICK) fold that provides resistance to chemical and thermal degradation1.
There are nine mammalian subtypes of voltage-gated NaV channels: They are responsible for propagating action potentials in excitable cells and are considered to be important therapeutic targets for a wide variety of pathophysiological conditions such as cardiac arrhythmia, and epilepsy. NaV1.7 channel plays an important role in the human pain signaling pathway and it is an important therapeutic target for treatment of chronic pain1,2.
Phlo1b (#STP-370) is a highly pure, synthetic, and biologically active peptide toxin.
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