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 (Periplanela 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. (C) 2003 Elsevier Science (USA). All rights reserved.
Massilia, G.r., Eliseo, T., Grolleau, F., Lapied, B., Barbier, J., Bournaud, R., et al. (2003). Contryphan-Vn: a modulator of Ca2+-dependent K+ channels RID A-4573-2009. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 303(1), 238-246 [10.1016/S0006-291X(03)00331-0 WC Biochemistry & Molecular Biology; Biophysics].
Contryphan-Vn: a modulator of Ca2+-dependent K+ channels RID A-4573-2009
POLTICELLI, Fabio
2003-01-01
Abstract
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 (Periplanela 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. (C) 2003 Elsevier Science (USA). All rights reserved.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
