Sodium channel modulating activity in a delta-conotoxin from an Indian marine snail
| Autor: | S. Sudarslal, Prajna P Pal, Siddhartha P. Sarma, K. S. Krishnan, P. Ramasamy, Ritu Dhawan, Anil K. Lala, Sriparna Majumdar, Padmanabhan Balaram, Mani Ramaswami, Sujit Kumar Sikdar |
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| Rok vydání: | 2003 |
| Předmět: |
Spectrometry
Mass Electrospray Ionization Molecular Sequence Data Snails Biophysics India Peptide Conus amadis Venom Snail Biology Biochemistry Sodium Channels Structural Biology biology.animal Genetics Animals Conotoxin Amino Acid Sequence Molecular Biology Peptide sequence Chromatography High Pressure Liquid chemistry.chemical_classification Mass spectrometry Sequence Homology Amino Acid Sodium channel Chinese hamster ovary cell Sodium Cell Biology biology.organism_classification δ-Conotoxin Electrophysiology Molecular Weight chemistry Conus peptide Conotoxins |
| Zdroj: | FEBS letters. 553(1-2) |
| ISSN: | 0014-5793 |
| Popis: | A 26 residue peptide (Am 2766) with the sequence CKQAGESCDIFSQNCCVG-TCAFICIE-NH(2) has been isolated and purified from the venom of the molluscivorous snail, Conus amadis, collected off the southeastern coast of India. Chemical modification and mass spectrometric studies establish that Am 2766 has three disulfide bridges. C-terminal amidation has been demonstrated by mass measurements on the C-terminal fragments obtained by proteolysis. Sequence alignments establish that Am 2766 belongs to the delta-conotoxin family. Am 2766 inhibits the decay of the sodium current in brain rNav1.2a voltage-gated Na(+) channel, stably expressed in Chinese hamster ovary cells. Unlike delta-conotoxins have previously been isolated from molluscivorous snails, Am 2766 inhibits inactivation of mammalian sodium channels. |
| Databáze: | OpenAIRE |
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