Therapeutic Protein Aggregation

Therapeutic proteins are one of the fastest-growing segments in the pharmaceutical industry.  A major challenge with these proteins is maintaining their physical stability during storage.  These proteins can aggregate, leading to loss of efficacy and the risk of adverse immune responses to the aggregated therapeutic.  To prevent aggregation, the proteins are formulated with various additives to maintain their physical stability.  A lack of mechanistic understanding of the influence of stabilizers on proteins means that the development of stabilizing formulations requires extensive trial and error.  In collaboration with Prof. David Volkin in the Department of Pharmaceutical Chemistry we are exploring the interrelationships between protein dynamics, excipients, and physical stability.  The long-term goal of this work is to develop new screening technologies and a more rational approach to the formulation of therapeutic proteins.  Shown below are the effects of the destabilizer arginine on the flexibility of an IgG1 monoclonal antibody. [Publication link]

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