High-throughput synthesis and cloning of genes encoding venom peptides
Motivated by the advancement of genomics and the urgent need of discovery of new molecules with therapeutic interest, as are venom peptides, high throughput pipelines ( have been developed to replace traditional approaches and protocols for synthetic gene synthesis and protein production Several high throughput platforms have been used in the past decade to identify conditions for soluble protein expression or for synthetic DNA production in large scale
High-throughput expression of animal venom toxins in Escherichia coli to generate a large library of oxidized disulphide-reticulated peptides for drug discovery
Animal venoms are complex molecular cocktails containing a wide range of biologically active disul-
phide-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.
Gene design, fusion technology and TEV cleavage conditions influence the purification of oxidized disulphide-rich venom peptides in <i>Escherichia coli</i>
This study reveals that E. coli is a convenient heterologous host for the expression of soluble and functional venom peptides. Using the optimal construct design, a large and diverse range of animal venom peptides were produced in the µM scale. These results open up new possibilities for the high-throughput production of recombinant disulphide-rich peptides in E. coli.