Synthesis of biologically active proteins as L6KD-SUMO fusions forming inclusion bodies in Escherichia coli.

A new platform has been developed to facilitate the production of biologically active proteins and peptides in Escherichia coli. The platform includes an N-terminal self-associating L KD peptide fused to the SUMO protein (small ubiquitin-like protein modifier) from the yeast Saccharomyces cerevisiae, which is known for its chaperone activity. The target proteins are fused at the C termini of the L KD-SUMO fusions, and the resulting three-component fusion proteins are synthesized and self-assembled in E.

Vaccine building 'kit': combining peptide bricks to elicit a desired immune response without adding an adjuvant.

Protein nanoparticles (NPs) can be used as vaccine platforms for target antigen presentation. To conduct a proof-of-concept study to demonstrate that an effective NP platform can be built based on a short self-assembling peptide (SAP) rather than a large self-assembling protein. SUMO-based protein fusions (SFs) containing an N-terminal SAP and a C-terminal antigen were designed, expressed in  and purified.