Contryphan-Vn: a modulator of Ca super(2+)-dependent K super(+) channels

Contryphan-Vn is a d-tryptophan-containing disulfide-constrained nonapeptide isolated from the venom of Conus ventricosus, the single Mediterranean cone snail species. The structure of the synthetic Contryphan-Vn has been determined by NMR spectroscopy. Unique among Contryphans, Contryphan-Vn displa...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2003-03, Vol.303 (1), p.238-246
Main Authors: Raybaudi Massilia, G, Eliseo, T, Grolleau, F, Lapied, B, Barbier, J, Bournaud, R, Molgo, J, Cicero, DO, Paci, M, Eugenia Schinina, M, Ascenzi, P, Polticelli, F
Format: Article
Language:English
Subjects:
contryphan
Conus ventricosus
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Summary:Contryphan-Vn is a d-tryptophan-containing disulfide-constrained nonapeptide isolated from the venom of Conus ventricosus, the single Mediterranean cone snail species. The structure of the synthetic Contryphan-Vn has been determined by NMR spectroscopy. Unique among Contryphans, Contryphan-Vn displays the peculiar presence of a Lys-Trp dyad, reminiscent of that observed in several voltage-gated K super(+) channel blockers. Electrophysiological experiments carried out on dorsal unpaired median neurons isolated from the cockroach (Periplaneta americana) nerve cord on rat fetal chromaffin cells indicate that Contryphan-Vn affects both voltage-gated and Ca super(2+)-dependent K super(+) channel activities, with composite and diversified effects in invertebrate and vertebrate systems. Voltage-gated and Ca super(2+)-dependent K super(+) channels represent the first functional target identified for a conopeptide of the Contryphan family. Furthermore, Contryphan-Vn is the first conopeptide known to modulate the activity of Ca super(2+)-dependent K super(+) channels.
ISSN:0006-291X
DOI:10.1016/S0006-291X(03)00331-0