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

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 pep tide described from a vermivorous species and the first purified from the v enom 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, i s amidated at the C-terminus, and maintains the five-residue intercystine l oop 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 Pro(4), and, remarkably, by the presence of the basic residue Lys(6) withi n 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. (C) 2001 Academic Press.