Short Courses*

Monday, November 4 2013, 9:00 - 12:30

SC1: Measures to Enhance Half-Life and Stability

Short Course Leaders:
Arne Skerra, Ph.D., Professor, Chair of Biological Chemistry, Technical University Munich; CEO, XL-protein GmbH
Javier Chaparro-Riggers, Ph.D., Associate Research Fellow, Protein Engineering, Rinat-Pfizer

This half-day workshop will provide an overview on the current state of the art in protein engineering, targeted at the improvement of half-life of antibodies and other proteins, which are key points to consider in the development of biopharmaceuticals. Current technologies to prolong the circulation of biologics, such as PEGylation, fusion with biological polymers (PASylation etc.), Ig Fc fusion and others will be covered and discussed.

• Renal filtration of biologics and the basics of pharmacokinetics (PK)
• Management of short plasma half-life, a problem of most biopharmaceuticals
• Current and new technologies to prolong the circulation of biologics: PEGylation vs.PASylation
• Short introduction into special aspects of antibody PK
• Increasing T(1/2) by decreasing non-specific elimination
• Increasing T(1/2) by decreasing antigen-specific elimination
• Application to Fc-fusion proteins: FcRn and pH switch

SC2: Measurement, Characterization and Impact of Impurities and Aggregates

Short Course Leader:
Tudor Arvinte, Ph.D., CEO, Therapeomic, Inc. and University of Geneva, Switzerland

Attend this half-day workshop to gain a critical overview of the available techniques for detection of aggregation and impurities (leachables) and how these methods can be applied. Delegates will learn about strategies for combining analytical methods (e.g. fluorescence spectroscopy and use of fluorescent dyes, field flow fractionation, Nanosight, flow imaging) to ensure detection of aggregates across a range of particle sizes. High throughput analysis (HTA) and high throughput formulation (HTF) platforms will be presented. Using case-studies, potential causes of aggregation and prevention strategies will be discussed.

• Causes and avoidance of impurities and aggregates
• Impact of impurities and leachables
• New technologies for characterization
• Prevention strategies
• Discussion to include experiences of the participants regarding aggregation

SC3: Alternate Display Technologies

Short Course Leader:
John Löfblom, Ph.D., Assistant Professor, Molecular Biotechnology, AlbaNova University Center, Royal Institute of Technology (KTH)

• Development of new display systems to address shortcomings of phage and yeast display
• Constructing libraries and assessing library quality
• Screening and selection methods for generation of new affinity proteins as well as for epitope mapping purposes
• Coverage of bacterial display, E. coli display, and ribosome display

SC4: Securing Patents on Products in the US

Short Course Leaders to be announced

Thursday, November 7 2013, 17:30-20:30

Dinner SC5: Troubleshooting and Engineering of Antibody Constructs

Short Course Leaders:
Jonas V. Schaefer, Ph.D., Head, High-Throughput Laboratory, Biochemistry, University of Zurich
Annemarie Honegger, Ph.D., Senior Scientist, Biochemistry, University of Zurich

Recombinant antibodies vary widely in their biophysical characteristics, from stable monomers to metastable aggregation-prone oligomers. In particular, antibody variable domains differ in their intrinsic thermodynamic stability and often require labor-intensive engineering. While most antibody engineering is performed with small antibody fragments, the majority of molecules in the clinics are still of the full-length IgG format. Thus it is critical to understand how the poor stability of individual variable domains not only limits the biophysical properties of small fragments, but also affects the production yield, stability and homogeneity of full-length IgGs containing these domains.

Attend this short course to:

• Recognize potentially troublesome antibody variable domain sequences
• Know how to choose the appropriate framework and to improve its stability while humanizing non-human antibodies
• Use structure-based engineering to optimize your antibody’s biophysical properties
• Optimize your choices of the best possible format for your antibody
• Improve your expression strategies for different immunoglobulin products