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Antibody-based therapeutics have progressed into expanded applications through engineering breakthroughs and computational initiatives. Novel designs are creating therapeutic antibodies that minimize unwanted properties while improving specificity and half life. This meeting explores the engineering techniques and supporting technologies that have brought about this new age of antibody therapeutics.
7:00 am Conference Registration
7:30 Breakfast Presentation (Sponsorship Opportunity Available) or Morning Coffee
8:15 Chairperson’s Opening Remarks
Opening Keynote Presentation
8:20 Adimab’s Novel Human Antibody Discovery Platform
Tillman U. Gerngross, Ph.D., Co-Founder & CEO, Adimab; Professor, Engineering, Dartmouth College
Thirty years after Millstein and Kohler generated the first monoclonal antibodies, there is an increasing commercial interest in improved technologies to discover and optimize fully human antibodies. We have developed an integrated platform for the discovery and optimization of full-length human IgGs in yeast. We report the design and construction of synthetic antibody libraries that recapitulate key features of the human pre-immune antibody repertoire. The platform typically yields hundreds of fully human IgGs in a matter of weeks. Several case studies will be presented.
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9:00 Expanding Chemical Diversity of Antibodies: Unnatural Amino Acids for Novel Antibody Functions
Vaughn Smider, M.D., Ph.D., Assistant Professor, Molecular Biology, The Scripps Research Institute
We have developed the technology to encode unnatural amino acids (UAAs) in antibody variable and constant domains. A phage display system has been developed that allows selection of scFv containing UAAs from combinatorial libraries. These unnatural variants and the technology to select them from libraries could open new target classes to recombinant antibodies. Additionally, unnatural amino acids in constant regions have allowed creation of site-specific immunoconjugates containing toxins, fluorophores, DNA, or even other proteins, opening a range of biochemical engineering options to the antibody field.
9:30 Phage Display Generation of Human Anti-Transferrin Receptor Cytotoxic Monovalent Antibody Fragments
Marie-Alix Poul, Ph.D., Group Leader, ENS Cachan-CNRS, Laboratoire de Biologie et Pharmacologie Appliquée
We have used phage display cell-based functional selections to isolate tumor specific internalizing antibodies. In this process, anti-transferrin receptor antibody fragments with high cytotoxic activity on various lymphoma and leukemia cell lines were generated. The mechanisms of cell cytotoxicity, which will be presented here, illustrate that the stringency of a functional selection permits the isolation of ligand-like binders with antagonistic effects.
10:00 Coffee Break, Exhibit and Poster Viewing
10:45 Design and Application of Antibody Cysteine Variants
Bernhard Helk, Ph.D., Section Head, Technology Development, Novartis Pharma AG
11:15 Impact of Post-Translational Modifications on Antibody Effector Functions
Shantha Raju, Ph.D., Assistant Director, Discovery Technology Research, Centocor R&D, Inc.
11:45 The Role of Technology and Sponsored by
Partnerships in the Development of a
First-in-Class Antibody Using the Virtual R&D Model
Alem Truneh, Ph.D., Co-Founder, CSO and Executive Vice President, R&D, NKT Therapeutics, Inc.
Combining advanced technologies and strong industry partnerships can speed the development of a first-in-class antibody therapeutic. A case study will be presented describing how NKT Therapeutics, in partnership with Selexis SA and others, rapidly progressed first-in-class antibodies targeting a highly specialized subset of T lymphocyte called iNKT cells to a stage of advanced pre-clinical development.
12:15 pm Close of Morning Session
12:30 Luncheon Presentations (Sponsorship Opportunities Available) or Lunch on Your Own
2:00 Chairperson’s Remarks
2:05 Energy-Based Analysis and Prediction of the Orientation between Light- and Heavy-Chain Antibody Variable Domains
Matthew P. Jacobson, Ph.D., Vice Chair, Pharmaceutical Chemistry; Associate Professor, WOS, Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco
Computer simulations play important roles in the design of small molecule drugs, but currently play a relatively small role in the design of antibodies. In this talk I will outline progress in predicting antibody structures from sequence, as well as related work from my lab on understanding the role of conformational flexibility in antibody recognition and optimizing antibody specificity. My goal is to stimulate discussion about the ways in which computer simulations can aid in the design of antibodies, including aspects such as pharmacokinetics which have received relatively little attention in the computational community.
2:35 Engineering Biotherapeutics for Reduced Immunogenicity
Gordon Webster, Ph.D., Co-Founder & Partner, Digital Biology Partners LLC
As regulatory agencies move towards de facto standards of immunogenicity safety for biotherapeutics, the pre-clinical assessment of potential immunogenicity will likely become mandatory. The ability to predict the presence of potential T-cell epitopes in proteins opens up the possibility of engineering them to reduce their immunogenicity and create safer and more effective biotherapeutics. The integration of immunogenicity prediction with the protein engineering process can significantly improve the chances of engineering a successful molecule with reduced immunogenicity and required pharmacological properties.
3:05 Engineered Antibodies and Molecular Imaging: Shedding Light on Drug Development
Anna Wu, Ph.D., Professor, Molecular & Medical Pharmacology; Associate Director, Crump Institute for Molecular Imaging, UCLA
Due to their highly selective binding properties, cancer-specific antibodies can form the basis of molecular imaging agents for in vivo detection of cell surface markers on tumors. Rapid targeting/rapid clearing fragments are highly suited for labeling with positron-emitting radionuclides (I-124, Cu-64, F-18), for imaging using positron-emission tomography (PET). Antibody-based imaging is highly translatable, and is poised to play a significant role in drug development, and ultimately in cancer diagnosis, staging, and treatment monitoring in the clinical setting.
3:35 Presentation to be Announced
3:50 Networking Refreshment Break
4:30 Structure-Based Prediction of Antibody Epitopes
Julia V. Ponomarenko, Ph.D., Senior Research Scientist, Computational Biology, Supercomputer Center, Skaggs School of Pharmacy & Pharmaceutical Science, University of California, San Diego
5:00 Mapping of Discontinuous Conformational Epitope by the Combination of Amide Hydrogen/Deuterium Exchange Mass Spectrometry and Docking
Yoshitomo Hamuro, Ph.D., Senior Director, H/D exchange, ExSAR Corporation
H/D-exchange epitope mapping technology can identify a discontinuous conformational epitope in a manner that reflects the solution state of the complex. It is a robust and widely-applicable analytical technique that can address obstacles common to alternative techniques. Furthermore, combining with computational docking, this method can yield high resolution models of antibody-antigen complexes, effectively predicting the actual contact residues on the antigen as verified by co-crystal analysis.
5:30 Reception in the Exhibit Hall
6:30 Close of Day