Contryphan-Vn: a novel peptide from the venom of the Mediterranean snail Conus ventricosus
| Autor: | Fabio Polticelli, Me Schinina, Paolo Ascenzi, Gr Massilia |
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| Rok vydání: | 2001 |
| Předmět: |
Models
Molecular Spectrometry Mass Electrospray Ionization Alkylation Protein Conformation Snails Static Electricity Biophysics Mollusk Venoms Peptide Venom Snail Biochemistry Peptides Cyclic Residue (chemistry) conus ventricosus biology.animal Conus peptide purification Mediterranean Sea Animals Amino Acid Sequence Molecular Biology Peptide sequence 3d model building mass spectrometry chemistry.chemical_classification Contryphan biology contryphan Tryptophan Cell Biology biology.organism_classification chemistry Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization |
| Zdroj: | Biochemical and biophysical research communications. 288(4) |
| ISSN: | 0006-291X |
| Popis: | 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 [formula] 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. |
| Databáze: | OpenAIRE |
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