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12:00 pm Registration
1:30 Chairperson’s Opening Remarks
1:40 OPENING KEYNOTE PRESENTATION
Emerging Mass Spectrometry-Based Tools to Characterize Higher Order Structure and Dynamics of Biopharmaceuticals
Igor A. Kaltashov, Ph.D., Associate Professor, Department of Chemistry, University of Massachusetts, Amherst
Among several MS-based techniques, targeting protein higher order structure and dynamics, hydrogen/deuterium exchange (HDX) has demonstrated the greatest promise vis-à-vis conformational analysis of biopharmaceutical products. Several examples of biopharmaceutical products (interferon beta 1a, velaglucerase, etc.) will be used to illustrate the utility of HDX MS and related techniques as a means of characterizing protein drugs in terms of their conformational integrity, stability and functional competence with high predictive value.
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2:10 Quantitative Method for Measurement of Antibody Internalization using Fluorescent Imaging
Inna Vainshtein, Ph.D., Scientist II, Global PK-PD & Bioanalysis, MedImmune
Quantitative assessment of internalization is important in development of antibody therapeutics. Despite a number of publications describing antibody-mediated receptor internalization, quantitative assessment of this process has not been extensively presented. Target-mediated internalization may increase antibody clearance and result in non-linear pharmacokinetic (PK) profiles. For immunotoxins, internalization could effect efficiency of toxin delivery into the target cells. We have developed a quantitative image-based method for measurement of antibody internalization. Examples will be presented to demonstrate the application of this methodology to development of therapeutic antibodies.
Sponsored by
2:40 Antibody Screening using Multiplexed SPR
Speaker to be Announced
2:55 Sponsored Presentation
To Be Announced
3:10 Refreshment Break, Poster and Exhibit Viewing
4:00 Combining Label Free Assay Platforms to Support Therapeutic Antibody Development from Identification of Candidate Antibodies through Pre-Clinical Development
Robin Barbour, Director, Antibody Technology, Elan Pharmaceuticals
Label free technologies can impact antibody development from the earliest phase through entry into the clinic and beyond. In this presentation, we compare and contrast three optically-based label free technologies, the Biacore T100, the Forte-Bio Octet, and SRU bind in their ability to screen antibodies from tissue culture supernatants and then to characterize the resultant positives for affinity, kinetics, epitope binding and domain binding. During the presentation, the advantages and disadvantages of each technology will be highlighted.
4:30 Proteomic Profiling of Novel Protein Targets by Selective Epitope Inhibition and SILAC/MS Analysis
Christian Freund, Ph.D., Principal Investigator/Group leader, Structural Biology, FMP/Free University of Berlin
We have a developed a rapid and robust method for addressing specificity of protein-protein interactions by a combined inhibitor/SILAC/MS approach. As exemplified by intracellular adaptor domains involved in disease processes, we show that deconvolution of epitopes is possible. This allows one to define the contribution of individual interaction sites for the assembly of molecular machines (e.g., the spliceosome) or signaling pathways.
5:00 End of Day
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