ASIC1a & 1b channel blocker

Mambalgin-1 was initially isolated by Sylvie Diochot and collaborators from the venom of the black mamba (Dendroaspis polylepis polylepis). Mambalgin-1 is a potent and selective blocker of acid-sensing ion channels (ASIC). ASIC channels have been demonstrated to be implied in pain pathways and appear to be promising therapeutic targets.  Mambalgin-1 rapidly and reversibly inhibits recombinant homomeric ASIC1a (IC50=55 nM) and heteromeric ASIC1a+ASIC2a (IC50=246 nM) or ASIC1a+ASIC2b channels (IC50=61 nM) but also human channels hASIC1b (IC50=192 nM) and  hASIC1a+hASIC1b (IC50=72nM).

Mambalgin-1 belongs to the family of three-finger toxins and has no sequence/structural homology with either PcTx1 or APETx2. Mambalgin-1 differs from mambalgin-2 by one amino acid. Both have demonstrated a similar activity. Mambalgin-1 has no effect on ASIC2a, ASIC3, ASIC1a+ASIC3 and ASIC1b+ASIC3 channels, as well as on TRPV1, P2X2, 5-HT3A, Nav1.8, Cav3.2 and Kv1.2 channels.

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Fig 1: Dose-response curve of the effect of synthetic Mambalgin-1 #MAM001 on ASIC1a current recorded in Xenopus oocytes. In this system, an IC50 of 21 nM was determined.

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Product code: MAM001. Category: . Tags: , , , , , .

Disulfide bonds: Cys3-Cys19, Cys12-Cys37, Cys41-Cys49, Cys50-Cys55
Length (aa): 57
Formula: C272H429N85O84S10
Molecular Weight:  6554.59 Da
Appearance: white lyophilized solid
Solubility: water or saline buffer
CAS number: not available
Source: synthetic
Purity rate: > 98 %


Black mamba venom peptides target acid-sensing ion channels to abolish pain.
Characterization of hASIC1a channels upon toxin mambalgin-1 binding in live mammalian cells
Binding site and inhibitory mechanism of the mambalgin-2