Bifunctional Hybrid Protein
The Bifunctional Hybrid Protein (BHP) technology platform is a highly convenient and functional research enabling tool for displaying protein polypeptide(s) or protein domain(s) of interest within the native structure of a β-Lactamase enzyme scaffold. The exogenously displayed polypeptide is reconstructed as a biologically active molecule. The fact that the exogenously displayed polypeptide is actually inserted into the enzyme scaffold avoids numerous pitfalls inherent in the techniques relying on fusion or chemical conjugation, and offers stability, reproducibility, uniformity and greater control of the final product.
As a result, BHP technology must be considered as a useful BioTool for protein domain studies.
Understanding the interaction sites of proteins and reconstructing these as biologically active molecules remains a critical challenge in drug discovery. Recreating the protein interaction sites in a spatial, constrained orientation that closely mimics the native protein structure is a real challenge and a difficult task to undertake. Protein interaction sites, once identified, are sometimes hard to manage at the laboratory level.
The core of the BHP technology is based on the use of an active-site serine β-lactamase enzyme as the protein scaffold. This enzyme catalyses the hydrolysis of the β-lactam ring of penicillin-related antibiotics. The insertion site is a highly permissive loop diametrically opposed to the site of enzyme activity. This ensures solvent accessibility for the exogenous polypeptide and limits the entering of steric hindrances into the active site of β-lactamase.
Scientists are always being dealing with quite complex proteins involved in intricate environment of interactions. Those proteins are sometimes unavailable as a functional and suitable material. Rather then use the whole protein of interest, the BHP technology allows the dissociation of the different structural elements of a protein. In this way, one simplifies the complexity of the protein-protein interaction environment and brings it into an easily-manageable unit, the BHP, for use in protein domain studies.
Our technologies have been validated by multiple research projects related to industrial final products.