Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-39438
Toxicon 2009 Jul 01;541:56-61. doi: 10.1016/j.toxicon.2009.03.014.
Show Gene links Show Anatomy links

Chemical synthesis and folding of APETx2, a potent and selective inhibitor of acid sensing ion channel 3.

Jensen JE , Durek T , Alewood PF , Adams DJ , King GF , Rash LD .


???displayArticle.abstract???
Acid sensing ion channels (ASICs) are pH-sensitive channels that are distributed in the central and peripheral nervous system and which are believed to play a key role in pain perception. APETx2, a 42-residue peptide toxin isolated from the sea anemone Anthopleura elegantissima, is the only known selective inhibitor of ASIC3 channels. Here we describe the total chemical synthesis of APETx2 by solid-phase peptide synthesis and native chemical ligation. The folded synthetic toxin had an IC(50) of 57 nM for inhibition of rat ASIC3 channels expressed in Xenopus oocytes, in agreement with the IC(50) reported for the native toxin (63 nM). The native chemical ligation approach should provide an efficient route for synthesis of other pharmacologically useful disulfide-rich toxins from venomous animals.

???displayArticle.pubmedLink??? 19306891
???displayArticle.link??? Toxicon


Species referenced: Xenopus laevis
Genes referenced: asic3