Isolation and characterization of a novel conus peptide with apparent antinociceptive activity
| Autor: | A Vyazovkina, Lourdes J. Cruz, Grzegorz Bulaj, Doju Yoshikami, James E. Garrett, G O Corpuz, J M McIntosh, Baldomero M. Olivera, John D. Wagstaff, Richard T. Layer |
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| Rok vydání: | 2000 |
| Předmět: |
Male
Hot Temperature Disulfide Linkage Stereochemistry Molecular Sequence Data Pain Venom Peptide In Vitro Techniques Receptors Nicotinic Biochemistry Mice Xenopus laevis Conus Animals Conotoxin Amino Acid Sequence Molecular Biology Peptide sequence Conus marmoreus chemistry.chemical_classification Analgesics biology Sequence Homology Amino Acid Rana pipiens Cell Biology biology.organism_classification Electric Stimulation Peptide Fragments Recombinant Proteins Protein Subunits Spinal Nerves chemistry Oocytes Conus Snail Conotoxins Sequence Alignment |
| Zdroj: | The Journal of biological chemistry. 275(42) |
| ISSN: | 0021-9258 |
| Popis: | Cone snails are tropical marine mollusks that envenomate prey with a complex mixture of neuropharmacologically active compounds. We report the discovery and biochemical characterization of a structurally unique peptide isolated from the venom of Conus marmoreus. The new peptide, mr10a, potently increased withdrawal latency in a hot plate assay (a test of analgesia) at intrathecal doses that do not produce motor impairment as measured by rotarod test. The sequence of mr10a is NGVCCGYKLCHOC, where O is 4-trans-hydroxyproline. This sequence is highly divergent from all other known conotoxins. Analysis of a cDNA clone encoding the toxin, however, indicates that it is a member of the recently described T-superfamily. Total chemical synthesis of the three possible disulfide arrangements of mr10a was achieved, and elution studies indicate that the native form has a disulfide connectivity of Cys1-Cys4 and Cys2-Cys3. This disulfide linkage is unprecedented among conotoxins and defines a new family of Conus peptides. |
| Databáze: | OpenAIRE |
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