Contryphan-Vn: A modulator of Ca2+-dependent K+ channels

Gabriella Raybaudi Massilia, Tommaso Eliseo, Francoise Grolleau, Bruno Lapied, Julien Barbier, Roland Bournaud, Jordi Molgó, Daniel Oscar Cicero, Maurizio Paci, Maria Eugenia Schininà, Paolo Ascenzi, Fabio Polticelli

Research output: Contribution to journalArticlepeer-review


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+ 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 Ca2+-dependent K+ channel activities, with composite and diversified effects in invertebrate and vertebrate systems. Voltage-gated and Ca2+-dependent K+ 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 Ca2+-dependent K+ channels.

Original languageEnglish
Pages (from-to)238-246
Number of pages9
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - Mar 28 2003


  • Ca -dependent K channels
  • Cockroach dorsal unpaired median neurons
  • Contryphan-Vn
  • Rat fetal chromaffin cells
  • Solution structure

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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