Applications of ion mobility mass spectrometry for characterization of protein therapeutics

Abstract

A major proportion of protein therapeutics marketed to date are produced by recombinant DNA technologies using well-chosen protein expression systems. Compared with small-molecule pharmaceuticals, recombinant therapeutic proteins are generally complex, heterogeneous, and subject to a variety of enzymatic or chemical modifications during expression, purification, and long-term storage. Because of unique structural features and production processes, the analytical strategies for characterization, quantitation, impurity profiling, and bioactivity evaluation of recombinant proteins represent a great challenge and a matter for debate.