title: Contryphan-Vn: a novel peptide from the venom of the Mediterranean snail Conus ventricosus.
abstract: 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 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 Pro(4), and, remarkably, by the presence of the basic residue Lys(6) 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.
authors.affiliation: Department of Biology, University "Roma Tre,", Viale G. Marconi 446, Rome, 00146, Italy.
authors.forename: G R
authors.initials: GR
authors.lastname: Massilia
authors.forename: M E
authors.initials: ME
authors.lastname: Schininà
authors.forename: P
authors.initials: P
authors.lastname: Ascenzi
authors.forename: F
authors.initials: F
authors.lastname: Polticelli
mesh_terms: D000478:Alkylation; D000595:Amino Acid Sequence; D000818:Animals; D008522:Mediterranean Sea; D008958:Models, Molecular; D008978:Mollusk Venoms / Q000737:chemistry*; D010456:Peptides, Cyclic / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D011487:Protein Conformation; D012908:Snails / Q000737:chemistry*; D021241:Spectrometry, Mass, Electrospray Ionization; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D055672:Static Electricity
chemical_list: D008978:Mollusk Venoms; D010456:Peptides, Cyclic; C102355:contryphan