Characterization of the structure and stability of human serum albumin isolated using a novel plasma extraction technique****

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Molecular chaperones are a highly interactive group of cellular proteins that fulfill central roles in all aspects of protein homeostasis including protein folding, assembly, and unfolding of substrates. Chaperones are typically categorized into families based on their sequence similarity and function. Another characteristic feature of molecular chaperones is their ability to suppress protein aggregation under stress conditions. In this regard, human serum albumin (HSA) acts like a chaperone protein preventing protein aggregation. HSA is one of the most abundant proteins in blood plasma. It is essential for the transport of free fatty acids, ions, bile salts and other compounds. It is also required to maintain the colloidal osmotic pressure in the body and provides the majority of plasma anti-oxidant activity. Importantly, the depletion of HSA from human plasma results in a large increase in protein aggregation under physiological stress conditions. ****In this Engage project, the Houry group will collaborate with Evolve Biologics to characterize the structure and function of HSA generated by the company's unique proprietary technology, termed 'PlasmaCap EBATM', to extract proteins from blood plasma. This novel technique has resulted in the extraction of more proteins at higher purity from each liter of donor plasma as compared to the legacy technology in the plasma products industry. The project represents a natural collaboration for the two groups, since the Houry group studies molecular chaperones using the latest biochemical, biophysical, and structural approaches, while Evolve Biologics has extensive experience in plasma proteins. ****One of Evolve Biologics' priorities is in developing and commercializing well-established plasma protein therapeutics, such as HSA. Hence, this collaboration will have direct translational benefits in improving people's health in Canada and worldwide dependent on plasma protein therapeutics.