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Structural Diversity and Basic/Acidic Residue Balance of Active Cysteine-Rich Insecticidal Peptides from Spiders

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Part of the book series: Toxinology ((TOXI))

Abstract

Among different cysteine-rich peptides produced by poisonous animals, the venom of spiders contains the most diverse cystine scaffolds with insecticidal activities but with a similar compact beta-sheet three-dimensional structure containing a significant amount of basic residues balanced with anionic ones, which could be substantial for both diffusion to the their cell target and binding to their protein receptors. The different cationic and anionic balance of the insecticidal spider peptides also suggests that other binding sites in the insect receptors could exist. Compared to the market and commercial pesticides, a minute selection of insect pests has been tested with the insecticidal spider toxins; however, they have shown strong activity against selected species of lepidopteran, dipteran, blattodean, and orthopteran with the inconvenience that the insecticidal peptides exert their lethal activity once injected into the hemolymph of insects. The knowledge on the precise targeting of insect receptors by robust ligands from spider venoms could be useful for understanding the molecular basis of toxin selectivity at the receptor level. This could also lead to the design of more effective and safer pesticides. This chapter addresses most of the insecticidal spider peptides already discovered with reported lethal or paralytic activity.

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Acknowledgments

This work was financed by grants from Dirección General de Asuntos del Personal Académico (DGAPA-UNAM), grant number IN204415, and SEP-CONACyT, grant number 240616.

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Correspondence to Gerardo Corzo .

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García, F., Villegas, E., Ortiz, E., Corzo, G. (2015). Structural Diversity and Basic/Acidic Residue Balance of Active Cysteine-Rich Insecticidal Peptides from Spiders. In: Gopalakrishnakone, P., Corzo, G., Diego-Garcia, E., de Lima, M. (eds) Spider Venoms. Toxinology. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-6646-4_2-1

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  • DOI: https://doi.org/10.1007/978-94-007-6646-4_2-1

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