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The second track of the Biotherapeutics Analytical Summit on Analytical Characterization of Biotherapeutics presents advances in analytical technologies using a range of products as examples including antibody-drug conjugates and bi-specifics. There is a focus on the characterization of particulates, host cell proteins and sequence variants, including an FDA presentation on particle characterization and product release limits. Additional sessions cover analysis of variants and the relationship between structure and function.
Tuesday, March 25
2:00 pm Chairperson’s Opening Remarks
Qin Zou, Ph.D., Senior Principal Scientist, Analytical Research & Development, Pfizer, Inc.
2:05 pm State-of-the-Art Mass Spectrometry Methods for Antibodies, Biosimilars, Bispecifics and ADC Characterization
Alain Beck, Ph.D., Senior Director, Antibody Physico-Chemistry, Centre d’Immunologie Pierre Fabre and Associate Editor, mAbs
The early use in the R&D process of Mass Spectrometry (MS) methods helps to optimize the structure and the function of next-generation mAbs (OptimAbs), as well as more sophisticated derivatives such as bispecific antibodies and antibody-drug conjugates (OptimADCs). These MS techniques are also very helpful for comparability studies and for biosimilarity evaluation. Case studies on deep structural characterization of antibodies and derivatives based on emerging methods such as middle-up/down, native and Ion-Mobility MS will be showcased and discussed.
2:35 pm TEM as an Analytical Characterization Tool for Biotherapeutics and other Protein Macromolecules
Bridget Carragher, Ph.D., Integrative Structural and Computational Biology, Scripps Research Institute
Transmission electron microscopy (TEM) is an emerging analytical tool for the characterization of proteins, protein complexes and submicron protein aggregates. Single particle EM (SPEM), can be used to reveal the architecture and dynamics of individual antibodies and antibody complexes, so as to understand their degree of conformational heterogeneity, and determine the binding sites between antibodies and antigens. The methods will be described and several case studies will be presented.
3:05 pm The Hunt for the Missing S: Detection, Control and Impact on Product Properties of Thioether Bonds in Fabs
John O’Hara, Ph.D., Director, Characterization & Method Development, Analytical Sciences, Biologicals, UCB
During a large scale GMP manufacturing campaign for a late stage development candidate a non-reducible species was detected on non-reducing SDS-PAGE. The characterization of this species resulted in the identification of a thioether bond. This presentation will review the characterization of the thioether bond as well as studies on the effect of process conditions on the levels of thioether. Finally, the impact of thioether bonds on the product quality and activity was assessed using a range of analytical techniques.
3:35 pm Improved Understanding of Association Between Protein Colloidal and Conformation Stability with Combined DLS/Raman
E. Neil Lewis, CTO, Malvern Instruments Limited
A novel technique for protein therapeutics characterization, specifically the combination of dynamic light scattering (DLS) and Raman spectroscopy in a single platform. This system simultaneously characterizes protein secondary and tertiary structure, as well as hydrodynamic size, even at high concentrations (> 50 mg/mL), enabling the link between colloidal and conformational stability to more fully understood. The new insights and observations gained by applying DLS/Raman to actual bio-pharmaceutical formulations will be shown.
4:05 pm Refreshment Break in the Exhibit Hall with Poster Viewing
4:30 pm Effective and Meaningful System Suitability Control for Sequence Variant Analysis
Melissa Alvarez, MS, Senior Research Associate, Protein Analytical Chemistry, Genentech, Inc., a member of the Roche group
Sequence variants in recombinant protein therapeutics are product-related variants arising from unintended amino acid substitutions. Peptide mapping LC-MS/MS is currently the method of choice for confirming sequence fidelity in protein products. To ensure the highest detection sensitivity and consistency during sequence variant analysis, a system suitability test was developed. The control sample and its use were designed to reflect the desired detection capability and to verify assay performance.
5:00 pm Analysis of Variants in PEGylated Proteins and their Non PEGylated Precursors
Jeffrey D. Meyer, Ph.D., Director, BioProcess Development, ZymoGenetics (a Bristol-Meyers Squibb Company)
PEGylated proteins pose unique analytical challenges. For the non-PEGylated form of a protein, efficient HPLC analyses can be developed to resolve charge and hydrophobic/hydrophilic variants. In contrast, the decrease in resolution upon PEGylation may necessitate analysis of the non-PEGyalted intermediates or the use of peptide maps. Further, PEGylation can lead to generation of new variants such as multiply PEGylated forms, dimeric forms arising from bifunctional dimeric PEG, and positional isomers.
5:30 pm End of Day One of Analytical Characterization
5:45 – 8:45 pm Dinner Short Courses*
SC1: Impurities: Measurement, Characterization and Impact
SC2: Glycobiology of Antibodies
* Separate registration required, click here for details
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