Towards a generic prototyping approach for therapeutically-relevant peptides and proteins in a cell-free translation system
Scientists from the Queensland University of Technology and the University of Queensland (Australia), with the participation of a member of the group of molecular tools for living system studies (IBCH), have developed a method that allows folding in vitro produced disulfide-rich peptides and proteins in an aggregation-free and thermodynamically controlled folding environment. To this end, we modify an E. coli-based in vitro translation system to allow co-translational capture of translated products by affinity matrix. This approach reduces aggregation of (poly) peptides and provides efficient oxidative folding under thermodynamic control. The developed approach can find application for prototyping a wide range of disulfide-constrained peptides, macrocyclic peptides with unnatural bonds, and antibody fragments in amounts sufficient for interaction analysis and biological activity assessment. The work was published in Nature Communications journal (IF 14.919).
january 14, 2022