Currently there are almost 40 therapeutic monoclonal antibodies approved for the treatment of a variety of diseases. These drugs are known for their efficiency in treatment due to their high selectivity; however, they are expensive to produce, and their effectiveness varies based on concentration in the patient’s bloodstream. Because of these issues, there arises a necessity for technology that provides cheaper and faster purification of antibodies during drug production, as well for technology that rapidly tests antibody concentrations in the bloodstreams of patients. In this lab, these problems are addressed using membranes modified with mimotopes, antigen like peptides, which selectively capture antibodies from solutions. The captured antibodies can be eluted as a purified product, or analyzed to determine the original concentration. While this membrane system has been successfully tested with the antibody Herceptin and its mimotope (K19), the system needs to be extended to additional therapeutic antibodies. Therefore, we tested whether the system successfully extends to the antibody Avastin and its mimotope (A19). However, the conformation of A19 varies greatly depending on small changes in pH which leads to significant amounts of non-specific binding. These conformational issues led to difficulties capturing Avastin, and the leaching of non-specifically bound A19 caused difficulties determining the amount of Avastin capable of being captured. The data collected thus far indicates that a different mimotope for Avastin may be more successful in binding large quantities of Avastin in a membrane.

In-membrane exploitation of antigen/antibody interaction for selective purification and quantification of therapeutic monoclonal antibodies

255th National Meeting (2018)

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