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Conformational stability and aggregation of therapeutic monoclonal antibodies studied with ANS and Thioflavin T

Veysel Kayser1, Naresh Chennamsetty, Vladimir Voynov

  • 1Chemical Engineering, Massachusetts Institute of Technology, Cambridge, MA, USA.

Mabs
|May 5, 2011
PubMed

Characterization of aggregation profiles of monoclonal antibodies (mAb) is gaining importance because an increasing number of mAb-based therapeutics are entering clinical studies and gaining marketing approval. To develop a successful formulation, it is imperative to identify the critical biochemical properties of each potential mAb drug candidate. We investigated the conformational change and aggregation of a human IgG1 using external dye-binding experiments with fluorescence spectroscopy and compared the aggregation profiles obtained to the results of size-exclusion chromatography. We show that using an appropriate dye at selected mAb concentration, unfolding or aggregation can be studied. In addition, dye-binding experiments may be used as conventional assays to study therapeutic mAb stability.

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