4 research outputs found
Temperature-induced unfolding, aggregation, and interaction of therapeutic monoclonal antibodies
Temperature-induced unfolding, aggregation, and interaction of therapeutic monoclonal antibodies
Exploring Chemical Space for new Substances to stabilize a therapeutic Monoclonal Antibody
The physical stability of therapeutic proteins is a major concern in the development of liquid protein formulations. The number of degrees of freedom to tweak a given protein’s stability is limited to pH, ionic strength and type and concentration of excipient. There are only very few, mostly similar excipients currently in use, limited to the short list of substances generally recognized as safe for human use by the FDA. Opposed to the limited number of molecules the formulation scientist has at hand to stabilize a protein, there is the vastness of chemical space which is hypothesized to consist of 1060 compounds. Its potential to stabilize proteins has never been explored systematically in the context of stabilization of therapeutic proteins. Here we present a screening strategy to discover new excipients to further stabilize an already stable formulation of a therapeutic antibody. We use our data to build a predictive model to evaluate the stabilizing potential of small molecules. We argue that prior to worrying about the hurdles of toxicity and approval of novel excipient candidates, it is mandatory to assess the actual potential hidden in the chemical space