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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.

1:30 pm Conference Registration

2:00 BuzZ Session A 

2:45 Refreshment Break, Exhibit Viewing and Poster Awards

3:30 BuzZ Session B 

4:15 End of Day

4:30 Dinner Short Courses 

7:00am  Conference Registration

7:30  Breakfast Presentation (Sponsorship Opportunity Available) or Morning Coffee

 Selection & Design 

8:15  Chairperson’s Opening Remarks

Anna Wu, Ph.D., Professor, Molecular & Medical Pharmacology; Associate Director, Crump Institute for Molecular Imaging, UCLA

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., Global Executive Director, Technology Development, Biologics/Process Sciences, Novartis Pharma AG

Antibodies are extensively used as research tools in molecular biology and as therapeutics in medicine. In many cases, antibodies are engineered to contain surface cysteines for the site-specific conjugation of payloads. Two of the most common issues associated with antibody cysteine variants are oligomerization and specificity of labeling. We have developed a method for generating cysteine variants that are stable and can be conjugated efficiently and specifically based on SAP (spatial aggregation propensity) technology. Conjugation sites are selected that display specific SAP values and are not in the vicinity of high-SAP regions. We demonstrate superior conjugation properties for a series of SAP-based IgG1 cysteine variants and propose applications of the variants.

11:15  Impact of Post-Translational Modifications on Antibody Effector Functions

Shantha Raju, Ph.D., Assistant Director, Discovery Technology Research, Centocor R&D, Inc.

Post-translational modifications such as glycosylation, oxidation, and deamidation can affect protein functions. IgGs are complex glycoproteins that are glycosylated in the Fc region and these glycans affect antibody effector functions. Oxidation of methionine residues in the CH2/CH3 domain can also affect antibody functions. Deamidation of asparagine residues present in the Fc may also affect antibody functions. This presentation illustrates the heterogeneity of post-translational modifications and their effect on IgGs functions.

11:45 Using Dip and Read Label-Free Assays for Rapid Antibody-Antigen Characterization

Brian R. Miller, Ph.D., Senior Scientist, Biogen Idec

We’ve incorporated ForteBio’s Octet systems into our protein engineering platform.  We routinely screen protein libraries expressed in E. coli for molecules displaying improved biophysical properties, and the Octet allows us to quickly triage based on affinity measurements on crude samples.  This allows us to winnow out molecules which have reduced binding to their targets.  In programs where we have multiple candidate MAb’s or FAb’s, the Octet allows us to rapidly perform cross-blocking assays in order to group the antibodies in to similar bins.  Finally, the Octet has become an indispensible tool for determining antibody titer for research scale production.

12:15pm  Close of Morning Session 
 
12:30  Luncheon Presentations (Sponsorship Opportunities Available) orLunch on Your Own

Enhancing Properties Through Powers of Prediction 

2:00 Chairperson’s Remarks

Shantha Raju, Ph.D., Assistant Director, Discovery Technology Research, Centocor R&D, Inc.

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  Predicting Antibody Binding Properties by Interrogation of Fully Human Libraries with Deep Sequencing

Tod Woolf, Ph.D., VP of Technology Development, X-BODY Biosciences

We employ X-BODY’s Protein Chain Reaction™ method for rapid cell-free generation of hMABs under mammalian folding conditions. Our human VH and VL libraries capture the natural antibody repertoire and can be screened for binding to targets on living cells. We present data showing that sequencing of thousands of hits can provide an early read on the function and specificity of lead candidates.

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.

Sponsored by
 3:35  VB6-845(r) Case Study: Using In Silico and In Vitro Tools For Preclinical Immunogenicity Assessment
Sofie Pattijn, Sr. Group Leader Immunology, Lonza
Combined in silico de-immunization and in vitro testing can provide a rapid and cost-effective solution for reducing or avoiding immunogenicity risk in therapeutic proteins. The VB6-845(r) case study illustrates how to successfully use this two-pronged approach.

3:50  Networking Refreshment Break

 Antibody Epitopes 

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

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Links to Companion Meetings

Recombinant Protein Therapeutics 

Antibody Drug Products