Monoclonal antibodies and other similar biotherapeutics are playing an ever more important role in the treatment of autoimmune diseases and cancers. It is predicted that within a few years, seven of the top ten pharmaceuticals will be antibodies.
Unfortunately, these proteins are extremely hard to characterize, due to an almost infinite number of variants, exacerbated by post translational modifications such as charge variance and aggregation. The number, type and location of glycans adds a further degree of complexity.
We discuss these difficulties and also the current technologies used to maximize separation capabilities and structural elucidation.
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