Utility of High-Throughput Biophysical Analysis of Protein Stability during Formulation Development and Comparability Assessments

This presentation will examine both opportunities and potential pitfalls of utilizing high-throughput biophysical methods to assess protein stability during formulation development and comparability assessments of therapeutic proteins. The ability of various analytical methods to detect and monitor conformational changes and aggregate formation will be considered though the use of illustrative case studies including the characterization and stabilization of IgG1 and IgG2 mAbs, an albumin-fusion protein, and a recombinant version of a pentameric plasma glycoprotein. Data visualization techniques to analyze and summarize these large biophysical stability data sets will be discussed along with their usefulness for formulation development and potential applicability for comparability studies.