Successful refolding and NMR structure of rMagi3: A disulfide‐rich insecticidal spider toxin |
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Authors: | Gustavo Titaux‐Delgado Elisa Carrillo Angeles Mendoza Marlen Mayorga‐Flores Fátima C. Escobedo‐González Patricia Cano‐Sánchez Estuardo López‐Vera Gerardo Corzo Federico del Rio‐Portilla |
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Affiliation: | 1. Departamento de Química de Biomacromoléculas, Instituto de Química, Universidad Nacional Autónoma de México, CU, Ciudad de México, México;2. Laboratorio de Toxinología Marina, Unidad Académica de Ecología y Biodiversidad Acuática, Instituto de Ciencias del Mar y Limnología, Universidad Nacional Autónoma de México, Ciudad Universitaria, Ciudad de México, México;3. División de Ciencias e Ingenierías, Campus León, Universidad de Guanajuato, Loma del Bosque 103, Col. Lomas del Campestre León, Gto, México;4. Departamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, Universidad Nacional Autónoma de México, UNAM, Apartado Postal 510‐3, Cuernavaca, Morelos, México |
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Abstract: | The need for molecules with high specificity against noxious insects leads the search towards spider venoms that have evolved highly selective toxins for insect preys. In this respect, spiders as a highly diversified group of almost exclusive insect predators appear to possess infinite potential for the discovery of novel insect‐selective toxins. In 2003, a group of toxins was isolated from the spider Macrothele gigas and the amino acid sequence was reported. We obtained, by molecular biology techniques in a heterologous system, one of these toxins. Purification process was optimized by chromatographic methods to determine the three‐dimensional structure by nuclear magnetic resonance in solution, and, finally, their biological activity was tested. rMagi3 resulted to be a specific insect toxin with no effect on mice. |
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Keywords: | refolding disulfide‐bonded toxins NMR solution structure spider toxin insecticidal Macrothele gigas |
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