Amino Acid Sequence Determination and Chemical Synthesis of CllErg1 (γ-KTx1.5), a K+ Channel Blocker Peptide Isolated from the Scorpion Centruroides limpidus limpidus
A novel toxin named CllErg1 (systematic nomenclature γ-KTx1.5) was purified from the venomof the scorpion Centruroides limpidus limpidus and its amino acid sequence was determined. It has42 amino-acid residues cross-linked by four disulfide bridges and blocks specifically a potassiumchannel...
| Autores: | , , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2005 |
| País: | México |
| Institución: | Universidad Nacional Autónoma de México |
| Repositorio: | Redalyc-UNAM |
| OAI Identifier: | oai:redalyc.org:47549214 |
| Acceso en línea: | https://www.redalyc.org/articulo.oa?id=47549214 |
| Access Level: | acceso abierto |
| Palabra clave: | Química K+ ERG channel scorpion toxin chemical synthesis |
| Sumario: | A novel toxin named CllErg1 (systematic nomenclature γ-KTx1.5) was purified from the venomof the scorpion Centruroides limpidus limpidus and its amino acid sequence was determined. It has42 amino-acid residues cross-linked by four disulfide bridges and blocks specifically a potassiumchannel of the family ether-a-go-go (ERG). The full peptide was chemically synthesized and properlyfolded, showing that it blocks the human ERG-channels (HERG) with identical affinity to that of thenative peptide. Synthetic CllErg1 can be produced in quantities enough to compensate its lowconcentration in the natural venom. It paves the way to conduct studies aimed at the identification ofthe structural motifs of HERG critical for proper channel function. Additionally, another analogouspeptide CllErg2 (systematic name γ-KTx4.1) was purified and had its full amino acid sequencedetermined. It contained 43 amino acid residues, maintained closely packed by four disulfide bridges. |
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