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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- 作者：Jeremy Turchetto ; Ana Filipa Sequeira ; Laurie Ramond230
- 关键词：Venom peptides ; Disulphide bonds ; Periplasm ; Escherichia coli (E. coli) ; Drug discovery library ; High ; throughput production
- 刊名：Microbial Cell Factories
- 出版年：2017
- 出版时间：December 2017
- 年：2017
- 卷：16
- 期：1
- 全文大小：2459KB
- 刊物类别：Chemistry and Materials Science
- 刊物主题：Applied Microbiology; Biotechnology; Microbiology; Microbial Genetics and Genomics; Enzymology; Genetic Engineering;
- 出版者：BioMed Central
- ISSN：1475-2859
- 卷排序：16
文摘
BackgroundAnimal 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.