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THURSDAY, MAY 20

 

12:00 pm Registration

Emerging Tools & Technologies

1:30 Chairperson’s Opening Remarks

1:40 OPENING KEYNOTE PRESENTATION

Igor A. KaltashovEmerging 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. 

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
Biorad
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


Short Courses | Day 1 | Day 2 | Download Brochure





Program Navigation

Phage and Yeast Display of Antibodies and Proteins Engineering Antibodies Antibody Optimization Difficult to Express Proteins Pre-Clinical/Clinical Development Revival of Bispecific Antibodies Immunogenicity of Therapeutic Biologics Protein Aggregation in Biopharmaceutical Products Biotherapeutic Targets


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