Scientists in Singapore have developed a bacterial protein nanoparticle that correctly folds recombinant proteins, increases functional expression yields up to 100-fold, and shields the internalized proteins from damage by heat, chemicals, and proteolysis. Scientists at the National University of Singapore (NUS), and the Nanyang Technological University, who developed the thermostable exoshell (tES), hope that the technology could help to address some of the problems with recombinant protein production, both for research and industrial applications.
“Our findings highlight the potential of using highly engineered nanometer-sized shells as a synthetic biology tool to dramatically affect the production and stability of recombinant proteins,” claims lead researcher Chester Drum, M.D., Ph.D., assistant professor at the departments of medicine and biochemistry, at NUS Medicine, who is also a consultant cardiologist at the National University Hospital and director of the Clinical Trial Innovation Lab at the Translational Laboratory in Genetic Medicine (TLGM), A*STAR.
The team reports on development of the tES in Nature Communications (“Thermostable Exoshells Fold and Stabilize Recombinant Proteins”).
Expressing and stabilizing functional recombinant proteins remains a key challenge for both basic and industrial biology, the authors note. Technologies for improving protein folding, which range from chaperone co-expression to chemically engineered hydrogels, have had “varied success.” Methods for stabilizing protein products, including chemical cross-linking, rational mutagenesis, and directed evolution approaches, have also been applied both for basic and industrial applications.
Protective Thermostable Protein Exoshell Boosts Recombinant Protein Yield 100-Fold
