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Stabilization and Formulation of Therapeutic Proteins- Converting Molecules into Drugs:
Protein-based pharmaceuticals are the fastest-growing class of new drugs. They not only offer promise for treatments to address major health challenges such as cancer, but also a wealth of new engineering problems to solve. Chemical engineers have long been proficient at producing products that meet exacting specifications for chemical purity, but therapeutic proteins now bring additional challenges: these products must not only be highly chemically pure, but also conformationally pure, and must remain so after manufacturing through the drug’s entire shelf-life and delivery to patients. For economic viability, therapeutic protein formulations typically require a shelf life of 18-24 months. Over the course of this time the protein must retain adequate chemical and conformational purity. Meeting the stringent requirements for chemical and conformational stability during shelf life is a daunting task. Most of the common chemical degradation products (especially hydrolysis and oxidation byproducts) are significantly thermodynamically favored versus the desired native state of the protein. Furthermore, the properly folded native state of most proteins is only marginally more stable (the free energy of unfolding, ΔGunf, is about 20-60 kJ/mol) than the unfolded state, and appears to be unstable under most conditions with respect to aggregated forms of the protein.
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