A biologically active hydrophobic T-1-conotoxin from the venom of Conus spurius
| Autor: | Leticia Lezama-Monfil, Edgar P. Heimer de la Cotera, María Maillo, Heriberto Pedraza-Lara, Manuel B. Aguilar, Estuardo López-Vera |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
Physiology
Mollusk Venoms Peptide Motor Activity Mass spectrometry Biochemistry Peptides Cyclic Conus spurius Cellular and Molecular Neuroscience Mice Endocrinology Animals Conotoxin Amino Acid Sequence Peptide sequence chemistry.chemical_classification Chromatography Edman degradation biology Behavior Animal Protein primary structure Conus Snail biology.organism_classification Molecular Weight chemistry Monoisotopic mass Conotoxins Hydrophobic and Hydrophilic Interactions |
| Zdroj: | Peptides. 27(3) |
| ISSN: | 0196-9781 |
| Popis: | A major, very hydrophobic peptide, sr5a, was purified from the venom duct of Conus spurius specimens collected in the Yucatan Channel, Mexico. Its amino acid sequence (IINWCCLIFYQCC; calculated monoisotopic mass assuming two disulfide bridges 1616.68 Da) was determined by automatic Edman degradation after reduction and alkylation, and confirmed by mass spectrometry (ESI monoisotopic mass, 1616.60; MALDI monoisotopic mass 1616.42 Da). The primary structure of sr5a showed the pattern that characterizes the family of the T-1-conotoxins, which belong to the T-superfamily of conotoxins. The disulfide bonds were determined by partial reduction and alkylation with N-ethylmaleimide, followed by total reduction and alkylation with 4-vinylpyridine, and automatic Edman sequencing. The connectivity of the Cys residues (I-III, II-IV) is the same as that found in the T-1-conotoxin family. When injected intracranially (2.0 nmol) into mice, peptide sr5a caused depressed behavioral activity. |
| Databáze: | OpenAIRE |
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