Protein stability assays are necessary to assess critical quality attributes (CQAs). Long-term stability studies often include stressing biotherapeutics under conditions such as elevated temperature and pH to accelerate degradation and exacerbate differences in structure. This, in tandem with ion mobility-mass spectrometry (IM-MS) and collision induced unfolding (CIU), can allow us to analyze and assess stability differences of various biotherapeutics.
Example data of a thermal stress study of a monoclonal antibody (mAb). A mAb was heated for 4 weeks, with an aliquot collected at two weeks. Differences in CIU50 voltages are observed which is indicative of stability changes due to thermal stress.
For additional information, please refer to Kang, J. et al., Anal Bioanal Chem, 2020, 412(3).
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