1H NMR structural analysis of novel potassium blocking toxins using a nano-NMR probe.
A new class of toxin acting on potassium channels and cross-linked by four disulfide bridges instead of three has been recently described. Two peptides, Pi1 and Pi7, purified from the venom of the scorpion Pandinus imperator belong to this new class. Structural features of one of these new toxins. Pi1, have been investigated by proton nuclear magnetic resonance using a new technology that allows to work with very small amount of compound, in the nanomole range. It is shown that it is possible to collect high quality data set in terms of resolution, lineshape and sensitivity with nanomolar amount of compound using this technology. Preliminary results on Pi7 are also presented. The approach described here is quite attractive for the study of natural compounds such as toxins often available at low amounts.
Delepierre
M
M
Laboratoire de RMN Institut Pasteur, CNRS URA 1129, Paris, France.
Prochnicka-Chalufour
A
A
Possani
L D
LD
D000595:Amino Acid Sequence; D000818:Animals; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D026902:Potassium Channel Blockers; D011487:Protein Conformation; D012604:Scorpion Venoms / Q000737:chemistry* / Q000633:toxicity; D012605:Scorpions; D017386:Sequence Homology, Amino Acid
C104751:Pi1 toxin; C114246:Pi7 peptide; D026902:Potassium Channel Blockers; D012604:Scorpion Venoms