Cone snails (genus Conus) venoms are a rich source of small peptide toxins (conotoxins) that are of growing pharmaceutical importance. Yet conotoxins often prove costly and difficult to synthesize. Conotoxins commonly contain disulfide bonds that are critical for adopting correct structures. Formation of the correct disulfide bonds enhances the difficulty in synthesis. Here, recombinant expression in a modified Escherichia coli system was used. Fusion proteins with and without native E. coli DsbC (a disulfide bond isomerase) as well a cone snail specific protein disulfide isomerase were created. Several toxins were cloned into the fusion protein vectors. Results indicated that the toxins were expressed in high yields. Purification for subsequent functional studies is in progress.

Recombinant expression of conotoxins in Escherichia coli

2019 Spring National Meeting

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.