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Cambridge Healthtech Institute’s Inaugural
Turning Antibodies into Drug Products
Protein Science Impacts on the Progression from Discovery to Biotherapeutic Product
January 16-17, 2014


Following lead selection, an antibody drug candidate will navigate a complex path of steps leading to its readiness for an IND approval, first in man clinical studies and then ultimately its maturity into a drug product appropriate for phase 3 trials and commercial use. New disease indications, multispecific targeting and conjugates bring new challenges to preclinical studies, and the industry continues to push for new screening and design approaches that will accelerate and reduce the cost of antibody drug development. Turning Antibodies into Drug Products examines exciting new findings in biotherapeutic screening, assay development and product optimization that support high-quality regulatory filings and the evolution of antibodies into competitive biotherapeutics.

Day 1 | Day 2 | Download Engineering Brochure | Speaker Biographies 

THURSDAY, JANUARY 16

1:00-1:45 pm Conference Registration

 

Antibody Developability 

2:00 Chairperson’s Opening Remarks

Mark Flory, Ph.D., Principal Scientist, Target Discovery and Validation, Igenica

 

Keynote Presentation

2:05 Developability Assessment of Therapeutic Antibodies – A Concept for Early Lead Selection

Thorsten LorenzThorsten Lorenz, Ph.D., Principal Scientist, Integrated Biologics Profiling, Novartis Pharma AG

Early lead selection of biotherapeutics during preclinical development requires careful characterization of a variety of molecule properties to lower the risk for encountering unexpected obstacles during technical development. This presentation will outline the workflow for candidate assessment and support of early lead selection by featuring highlights for various physicochemical profiling as well as pre-formulation assays applied in Integrated Biologics Profiling.

 

2:45 Microscale Assays for Screening Drug-Like Properties

Allan Capili, Ph.D., Scientist, Protein Biochemistry, Biogen Idec

3:15 An Antibody Engineering Platform for High-Throughput Candidate Screening, Engineering & Optimization

Lorenzo BenatuilLorenzo Benatuil, Ph.D., Senior Scientist, Biologics, Abbvie Bioresearch Center

High-throughput selection and screening of large antibody libraries need a robust data management and analysis platform able to track sequence evolution and aggregate assay data for hit and lead selection. We will present use cases to highlight the impact of incorporating appropriate bioinformatics tools and information management system on antibody generation by AbbVie’s in vitro display technologies.

3:45 Selected Oral Poster Presentation: Targeted Delivery into Sensory Neurons of a SNARE Protease Using a Single Chain Antibody (scFv) Against the Extracellular Domain of P2X3 Inhibits the Release of a Pain Mediator 

Hui Ma, Ph.D., Post-Doctoral Researcher, Biomedical Diagnostics Institute, Dublin City University, Ireland

4:00 Refreshment Break in the Exhibit Hall with Poster Viewing

4:45 New Algorithm for Screening Aggregation-Prone Regions in Antibodies and Other Proteins

Marco BlancoMarco Blanco, Ph.D., Postdoctoral Researcher, Chemical and Biomolecular Engineering, University of Delaware

A new algorithm is developed to accurately characterize the thermodynamics of protein aggregation by identifying specific residue-residue interactions. Aggregation-prone regions are captured by considering the individual contribution of each amino acid to the free-energy of self-association of hexapeptides based on hydrophobic, electrostatic, and steric interactions. The algorithm also provides “rules” in designing proteins for controlling aggregation, which are specific for solution conditions.

5:15 MAb-mAb Interactions Controlled by Buffer Species and Arginine Salts

Christopher van der WalleChristopher van der Walle, Ph.D., Principal Scientist, Development, MedImmune

Understanding protein-protein interactions in the context of reversible-self association (RSA) and aggregation is important to the development of robust monoclonal antibody (mAb) solution formulations. Light scattering techniques were used to investigate the effect of buffer species and arginine salt form on mAb RSA and aggregation propensity. The choice of buffer species profoundly effected mAb-mAb repulsive versus attractive interactions and arginine:glutamic acid had distinct stabilizing qualities over arginine hydrochloride.

5:45 Close of Day

 

Day 1 | Day 2 | Download Engineering Brochure | Speaker Biographies