High-throughput expression of animal venom toxins in Escherichia coli to generate a large library of oxidized disulphide-reticulated peptides for drug discovery

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Turchetto, Jeremy | Sequeira, Ana Filipa | Ramond, Laurie | Peysson, Fanny | Brás, Joana | Saez, Natalie | Duhoo, Yoan | Blémont, Marilyne | Guerreiro, Catarina | Quinton, Loïc | de Pauw, Edwin | Gilles, Nicolas | Darbon, Hervé | Fontes, Carlos | Vincentelli, Renaud

Edité par CCSD ; BioMed Central -

International audience. Animal venoms are complex molecular cocktails containing a wide range of biologically active disulphide-reticulated peptides that target, with high selectivity and efficacy, a variety of membrane receptors. Disulphide-reticulated peptides have evolved to display improved specificity, low immunogenicity and to show much higher resistance to degradation than linear peptides. These properties make venom peptides attractive candidates for drug development. However, recombinant expression of reticulated peptides containing disulphide bonds is challenging, especially when associated with the production of large libraries of bioactive molecules for drug screening. To date, as an alternative to artificial synthetic chemical libraries, no comprehensive recombinant libraries of natural venom peptides are accessible for high-throughput screening to identify novel therapeutics.

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