Contryphan-Vn: A novel peptide from the venom of the Mediterranean snail Conus ventricosus

G. R. Massilia, M. E. Schininà, P. Ascenzi, F. Polticelli

Research output: Contribution to journalArticlepeer-review


The isolation, purification, and biochemical characterization of the novel peptide Contryphan-Vn, extracted from the venom of the Mediterranean marine snail Conus ventricosus, is reported. Contryphan-Vn is the first Conus peptide described from a vermivorous species and the first purified from the venom of the single Mediterranean Conus species. The amino acid sequence of Contryphan-Vn is Gly-Asp-Cys-Pro-D-Trp-Lys-Pro-Trp-Cys-NH2. As with other contryphans, Contryphan-Vn contains a D-tryptophan residue, is amidated at the C-terminus, and maintains the five-residue intercystine loop size. However, Contryphan-Vn differs from the known contryphans by the insertion of the Asp residue at position 2, by the lack of hydroxylation of Pro4, and, remarkably, by the presence of the basic residue Lys6 within the intercystine loop. Although the biological function(s) of contryphans is still unknown, these characteristics suggest distinct molecular target(s) and/or function(s) for Contryphan-Vn.

Original languageEnglish
Pages (from-to)908-913
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number4
Publication statusPublished - Nov 9 2001


  • 3D model building
  • Contryphan
  • Conus ventricosus
  • Mass spectrometry
  • Peptide purification

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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