Design of functional modular protein-based nanoparticles (PNPs)

<p>The overexpression of bacterial recombinant genes results in protein misfolding usually leading to their aggregation into protein deposits called inclusion bodies (IBs). IBs composed from active proteins can be produced cost-efficiently and obtained as a relatively pure source of recombinant protein. Protein-based nanoparticles (PNPs) provide several advantages over inorganic nanoparticles including biocompatibility and biodegradability. PNPs also show defined structure, mechanical stability and are amenable for surface alterations via genetic manipulation. Similarly, IBs also display several of these properties and as such they can be considered as ideal candidates for the design of PNPs with new functionalities. </p> <p>The p40 protein domain was first reported as an unknown domain of the multidomain β- mannanase enzyme (ManA) from the thermophilic bacterium Caldibacillus cellulovorans. Past attempts to recombinantly produced p40 in Escherichia coli resulted in the formation of insoluble p40-IBs. This project attempts to exploit the aggregating property of p40 and its tendency to form IBs to develop p40 as a PNP platform for biotechnological applications. </p> <p>The project explores the design of new modular proteins structures that contain at least two functionally distinct regions; (a) an aggregating part capable of forming insoluble p40-PNPs and (b) a biomolecule (e.g., enzyme, peptide, fluorescent protein) displayed on p40-PNPs. </p>