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Conference Short Courses* - View Details
Sunday, January 9 - 3:00 pm - 6:00 pm
Characterization and Analysis of Particulates
Protein Crystallization - Delineating Protein Structure
DoE and QbD: Tools for Optimizing the Bioprocess
Tuesday, January 11 - 4:30 pm - 7:30 pm
Thursday, January 13 - 6:30 pm - 9:00 pm
1:00 pm Conference Registration
1:45 Chairperson’s Opening Remarks
Ramil Latypov, Ph.D., Senior Scientist, Process and Product Development, Amgen, Inc.
1:50 Coping with the Colloidal Properties of Proteins
Thomas M. Laue, Ph.D., Professor, Biochemistry and Molecular Biology; Director, Biomolecular Interaction Technologies Center (BITC), University of New Hampshire
Often it is useful to consider the colloidal properties of a protein when considering how best to formulate it. This talk will describe the colloidal properties of proteins and how the solvent can be used to optimize solubility and viscosity. Experimental approaches will be described that are useful for determining the colloidal properties. The audience will gain a systematic understanding of the colloidal properties of proteins; ways to measure those properties; and guides for how solvent properties can influence the colloidal properties.
2:20 Novel Oxidative and Photolytic Pathways of Protein Degradation
Christian Schoneich, Ph.D., Professor, Chair, Department of Pharmaceutical Chemistry, University of Kansas
Protein aggregation and fragmentation represent important degradation pathways with potential long-term consequences such as immunogenicity. Here, we will present a series of novel degradation pathways of pharmaceutically relevant proteins such as immunoglobulins and growth hormone originating from Cys oxidation and/or disulfide reduction and photolysis, which ultimately form chemically stable ether and thioether cross-links. A mechanistic analysis of these pathways was performed with specifically designed model peptides.
2:50 Aggregation and Self-Association in a High Concentration Antibody Solutions
Devendra (Davy) S. Kalonia, Ph.D., Professor of Pharmaceutics, University of Connecticut
This talk will focus on the importance of solution properties of a monoclonal antibody at high concentrations. The effect of pH and ionic strength on self association and aggregation depends on the nature of the protein-protein interactions in solution. Application and limitations of multiple techniques to measure protein-protein interactions will also be discussed.
3:20 Sponsored Presentation (Opportunity Available)
3:35 Refreshment Break, Exhibit and Poster Viewing
4:30 Measuring and Increasing Protein Stability
C. Nick Pace, Ph.D., Professor, Medical Biochemistry &Genetics; Biochemistry and Biophysics, Texas A&M
Increasing conformational stability of proteins has been an important goal. I will discuss the methods that can be used to measure the conformational stability of proteins. In vitro selection has been used to increase protein stability, but most often site-directed mutagenesis is used to optimize the various forces that contribute to protein stability. I will discuss the most successful approaches based on site directed mutagenesis that can be used to stabilize proteins. In addition, I will discuss non-mutagenic approaches that can be used to stabilize proteins.
5:00 Towards Understanding Ion-Induced Protein Aggregation: Correlation with Biophysical Predictors of Stability
Yatin Gokarn, Ph.D., Associate Director, Late-Stage Pharmaceutical and Process Development, Genentech
The presentation will attempt to elucidate the underlying mechanism(s) governing ion-induced interactions in antibodies and related basic proteins. Case studies focused on studying the effect of ions on agitation and temperature induced aggregation and reversible self-assocation will be presented. The use of biophysical tools for predicting aggregation propensity and viscoelastic properties of mAbs will also be discussed.
5:30 Engineering, Characterizing and Formulating Aggregation-Resistant Antibodies
Peter M. Tessier, Ph.D., Assistant Professor, Department of Chemical & Biological Engineering, Center for Biotechnology & Interdisciplinary Studies, Rensselaer Polytechnic Institute
The significance of aggregation continues to grow with increasing demands for high concentration antibody formulations. We are pursuing three key approaches to address this problem: 1) Improve selection of antibodies; 2) reengineer existing antibodies; and 3) identify superior formulation conditions. Each of these ambitious pursuits is currently limited by the lack of understanding of how antibody sequence and structure influence aggregation, as well as a lack of high-throughput methods for identifying antibody variants or formulation conditions that minimize aggregation. In this presentation, we will discuss our work towards addressing each of these challenges.
6:00 Close of Day
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Links to Companion Meetings
Optimizing Biologics Formulation Development
Lyophilization, Spray Drying & Emerging Drying Technologies