Solubility Enhancing Fusion Proteins
Introduction Recombinant proteins having therapeutic, diagnostic or any other commercial or research applications are produced by expression in a host cell. However these proteins of interest are often misfolded and form insoluble aggregates known as inclusion bodies. Inclusion bodies are difficult to purify and are not suitable for work such as x-ray crystallography and enzymology which require the use of properly folded, soluble proteins. A number of methods to solve this problem have been developed including the use of fusion partners to make the protein more stable. Technology description Researchers at the University of Washington have developed a novel method for the production of recombinant proteins in a host cell based on an artificially designed rapidly folding fusion protein partner. The use of the fast folding fusion partner enhances the production of soluble protein of interest, minimizes the formation of insoluble aggregates and increases the protein expression levels. When combined with a protein of limited solubility, as in a fusion protein construct, the rapidly folding partner can induce the fusion protein to be soluble. This allows for expression of soluble proteins in E. coli which were formerly only made as inclusion bodies. Business opportunity This invention is useful for the production of recombinant proteins for research, therapeutics and industrial applications. The therapeutic protein production market now exceeds US$20 billion worldwide annually. In addition, this technology has wide applications in Structural Genomics for the production of large number of soluble proteins for x-ray crystallography.Type of Offer: Licensing
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