TAILIEUCHUNG - Báo cáo khoa học: Synthesis and characterization of Pi4, a scorpion toxin from Pandinus imperator that acts on K+ channels

Pi4 is a38-residue toxincross-linkedby fourdisulfidebridges that has been isolated from the venom of the Chactidae scorpion Pandinus imperator. Together with maurotoxin, Pi1, Pi7 andHsTx1, Pi4belongs to theaKTX6 subfamilyof short four-disulfide-bridged scorpion toxins acting on K + channels. Due to its very low abundance in venom, Pi4 was chemically synthesized in order to better characterize its pharmacology and structural properties. An enzyme-based cleavage of synthetic Pi4 (sPi4) indicated half-cystine pair-ings betweenCys6–Cys27, Cys12–32, Cys16–34 andCys22– 37, which denotes a conventional pattern of scorpion toxin reticulation (Pi1/HsTx1 type) | Eur. J. Biochem. 270 3583-3592 2003 FEBS 2003 doi Synthesis and characterization of Pi4 a scorpion toxin from Pandinus imperator that acts on K channels Sarrah M Barek1. Amor Mosbah1 Guillaume Sandoz2 Ziad Failoun1. Timoteo Olamendi-Portuaal3 Herve Rochat1. Francois Samnieri1 J. Inaki Guiiarro4. Pascal Mansuelle1 Muriel Delenierre4 B Michel De Waard2 and Jean-Marc Sabatier1 1 Laboratoire International Associé d Ingenierie Biomoléculaire et Laboratoire de Biochimie CNRS UMR 6560 LFR Jean Roche Faculti de Medeciru Nord Mareeille Faance 2Laboratoire Canaux loniques et Signalization Equipe mixte CNSERM 99-2 CEA Glanoble Faanee 3Iostitute of Biotechnology National Autonomous Univeritty of Mxxico. Cuemaeaea Mexico 4Unite de RMN des Biomolicules Dépt. de Biochimie Structurale et Chimie nnsittut Fasten CNRS 2155 11 9 Frmce Pi4 is a 38-residue toxin cross-linked by four disulfide bridges that has been isolated from the venom of the 0 x10 11 scorpion Pandinus impleatoe. Together with maurotoxin Pi1 Pi7 andHsTx1 Pi4 belongs to the a KTX6 subfamily of short four-disulfide-bridged scorpion toxins acting on K channels. Due to its very low abundance in venom Pi4 was chemically synthesized in order to better characterize its pharmacology and structural properties. An enzyme-based cleavage of synthetic Pi4 sPi4 indicated half-cystine pairings between Cys6-Cys27 Cys12-32 Cys16-34 and Cys22-37 which denotes a conventional pattern of scorpion toxin reticulation Pi1 HsTx1 type . In vivo sPi4 was lethal after intracerebroventricular injection to mice LD50 of Ig per mouse . In vitro addition of sPi4 onto Xenopus lawis oocytes heterologously expressing various voltage-gated K channel subtypes showed potent inhibition of currents from rat IC50 of 8 pM and Shaker B IC50 of 3 nM channels whereas no effect was observed on rat and channels. The sPi4 was also found to compete with 125I-labeled apamin for binding to small-conductance .

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