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Wednesday, May 19

7:00 am Registration and Morning Coffee


8:30 Chairperson’s Opening Remarks

George Georgiou, Ph.D., Professor, Chemical Engineering, University of Texas, Austin

8:40 Unique Combination of Computational Modeling, Antibody Engineering and Cell Biology

Birgit Schoeberl, Ph.D., Vice President, Discovery, Merrimack Pharmaceuticals

We will discuss the importance of disease context with respect to the design of monoclonal or bispecific antibodies. In addition, we will address the importance of growth factor receptor signaling crosstalk and how these insights drive the antibody design and engineering.

9:10 Importance of Early and Complete Characterization of Antibodies in the Lead Selection Process

Shrikant Deshpande, Ph.D., Senior Director, Protein Chemistry, Medarex, a wholly owned subsidiary of Bristol-Myers Squibb Co.

Selection of a lead candidate from a pool of antibodies is a critical step in product development. A wrong lead selected will result in major development issues. Understanding the biophysical and analytical characteristics of a pool of antibodies using a variety of tests will not only help select ideal leads, but also reduce or eliminate development issues.

9:40 Case Study: Engineered Human Antibody CH2 Constant Domains (Nanoantibodies) as Novel Candidate Therapeutics

Rui Gong, Ph.D., Postdoctoral Visiting Fellow, Protein Interaction Group, CCRNP, CCR, NCI-Frederick

Isolated immunoglobulin constant CH2 domains (nanoantibodies) are promising as scaffolds for selection of binders with potential effector functions. The binders against HIV-1 were selected and identified from several large libraries based on CH2 scaffold. However, CH2 domain is relatively unstable to thermally induced unfolding, which limits the use of CH2 as scaffold. A stabilized CH2 mutant (m01) with an additional disulfide bond was engineered and characterized, which can be used for the development of candidate therapeutic antibodies with increased stability.

10:10 Coffee Break, Poster and Exhibit Viewing

11:10 A Computational-Experimental Strategy for the Isolation of Antigen-Specific Antibodies from Immunized Animals

George Georgiou, Ph.D., Professor, Chemical Engineering, University of Texas, Austin

We have developed a computational-experimental strategy for the isolation of antigen-specific antibodies from immunized animals. This methodology is simple, fast and requires neither cloning nor screening. In addition, and to complement Ab isolation from immunized animals we have developed an improved bacterial display system for affinity maturation, for Fc engineering and de novo antibody discovery. 

11:40 Analytical Methods to Characterize and Evaluate the Mode of Action of Antibody Drug Conjugates

Vangipuram Rangan, Ph.D., Director, Protein Chemistry, Medarex, a wholly owned subsidiary of Bristol-Myers Squibb Co.

Antibody drug conjugates (ADC) are emerging platform technology where antibodies are used as targeting agents to deliver payloads to the tumor site. In order to characterize ADCs as well as to understand their mechanism of action, one has to develop various analytical methods and assays that are unique to ADCs. This presentation describes several analytical methods that are employed to characterize ADCs being developed at Medarex, a wholly owned subsidiary of BMS.

Sponsored by
12:10 pm Luncheon Presentation I

Slonomics® - An Innovative Toolbox for the Precise Engineering of Immunoglobulin Repertoires

Thomas Waldmann, Ph.D., Director, Science & Technology Support, Sloning BioTechnology GmbH

Slonomics®, a proprietary genetic engineering platform, uses standardized DNA triplets as building blocks. It allows for introducing multiple codons in parallel at any desired sequence position. The ability to precisely control the individual frequency of up to 20 specific codons per position results in genetically diverse libraries with unique molecular profiles. The technology easily allows for combining complex positional mutation strategies with diversifying the length of randomized regions. Therefore, synthetic antibody libraries of highest quality can be created that mimic the design of naturally occurring immunoglobulin repertoires.

Sponsored by

12:40 Luncheon Presentation II
Best Practices in the Design of Antibody Models Using In-Silico Methods.
Francisco G. Hernandez-Guzman, Ph.D., Product Manager, Life Sciences, Accelrys, Inc.
As the pharmaceutical, biotech and academic labs continue their research in antibodies as alternative therapeutic agents to classical small molecule therapy, more and more scientists are looking for structural information to help their understanding of antibody-antigen interactions, as well as various other biophysical properties. By leveraging the high homology within the antibody family, one can successfully build reliable models with a high degree of molecular detail. In this presentation, we will explore the process of building a homology for an Fab domain. We will highlight a process that has shown to give high quality models and we will discuss some of the challenges that one has to watch for during the model building process. We will also emphasize methodologies used to refine the Complimentary Determining Regions (CDRs) of the antibody, and in particularly explore some approaches that can be used to increase the reliability of modeling the challenging H3 loop.



1:30 Chairperson’s Remarks

Stefan Dübel, Ph.D., Professor, Technical Institute of Braunsweig

1:35 Application of H/D-Exchange for Epitope Screening to Assist with Candidate mAb Selection

Jennifer Nemeth, Ph.D., Principal Research Scientist, Biologics Research, Centocor Research and Development

Hydrogen/deuterium-exchange (H/D-Ex) coupled with mass spectrometry is having an impact in the biopharmaceutical arena in the area of epitope mapping and lead selection. As the use of the technology is still quite novel for biopharmaceutical applications, this talk is timely and relevant in this era of intelligent drug design. An example of the utility of this technology is highlighted during lead selection in a monoclonal antibody (mAb) drug program. As the timelines and sample amounts were limited, hydrogen/deuterium-exchange (H/D-Ex) was chosen for mapping out the epitopes on the target antigen, as opposed to more traditional techniques. Based on the results, lead and back-up mAbs were selected that had desirable epitopes for further product development.

2:05 High Throughput Selection and Comparison of Multimerization Strategies for Recombinant Antibodies

Stefan Dübel, Ph.D., Professor, Technical Institute of Braunsweig


Sponsored by
Forte Bio
2:35 Use of Disposable Label-Free Real-Time Biosensors in Epitope Binning Monoclonal Antibodies
Yasmina Noubia Abdiche, Ph.D., Senior Principal Scientist, Rinat Laboratories-Pfizer Inc.
This talk introduces a novel 384-well platform based on bio-layer interferometry (BLI) detection equipped with disposable fiber-optic tips that can be used for characterizing antibody interactions. Rerackable banks of 16 biosensors move to samples without any microfluidics, which opens up the possibility of immobilizing and regenerating batches of ligands on- or off-line to expedite screening. We compare data generated using BLI with those obtained by SPR to highlight the advantages of using this label-free real-time biosensor platform in the context of epitope binning monoclonal antibodies.


Sponsored by
2:50 Deriving and Epitope Mapping

Antibodies Targeting Membrane Proteins 

Benjamin Doranz, Ph.D., President and CSO, Integral Molecular

Integral Molecular’s Lipoparticle technology provides an innovative solution for presenting structurally intact membrane protein antigens, including GPCRs and ion channels, at concentrations 10-100x higher (50-200pmol/mg) than in cells or membrane preparations. This enabled us to derive high titer serum responses (>1:500) against membrane proteins of interest and to characterize resulting antibodies using techniques such as biosensor analysis. Once MAbs are isolated, our Shotgun Mutagenesis Mapping technology enabled us to rapidly identify both linear and conformationally complex epitopes that distinguish MAb binding sites.

3:15 Networking Refreshment Break, Poster and Exhibit Viewing

3:50 Problem Solving Break-Out Sessions

Table 1: in vitro screening or immunization? Isolating biologically active antibodies

Moderator: George Georgiou, Ph.D., Professor, Department of Biomedical Engineering, University of Texas at Austin


Table 2: CMC issues with ADCs

Moderator:  Vangipuram S. Rangan, Ph.D., Director, Protein Chemistry, Medarax Inc. a subsidiary of Bristol-Myers Squibb

  • Importance of identification of site of conjugation in current ADC platforms
  • Random conjugation versus site-specific conjugation
  • Importance of analytical methods

Table 3: Engineered Antibody Domains

Moderator: Rui Gong, Ph.D., Postdoctoral Visiting Fellow, Protein Interaction Group, CCRNP, CCR, NCI-Frederick

We and others have hypothesized that engineering of the antibody smallest independently folded fragments, the domains, with antigen-binding function could enhance access to targets and lead to highly potent broadly reactive inhibitors; such binders are much smaller (~ 10-fold) than immunoglobulin (Ig) Gs (IgGs) (even smaller than other Ig isotypes) and were termed engineered antibody domains (eAds). We have also hypothesized that the Ig heavy chain constant domain 2 (CH2) could be used as a scaffold to generate eAds that could mimic full-size antibody functions; they can also exhibit size-dependent functions and were termed nanoantibodies (nAbs).

  • How to increase the stability and solubility of the scaffolds - antibody domains.
  • How to increase the folding efficiency after introduction of foreign residues.
  • How to preserve or increase the stability of the eAds after grafting of foreign sequences.

Table 4: Increasing Efficiency of Phage Display Libraries and Selection

Moderator:  Prof. Dr. Stefan Dübel, Technische Universität Braunschweig, Institute of Biochemistry and Biotechnology

  • Pitfalls in library making
  • Controlling display valency
  • QC of libraries
  • Tuning of panning conditions to get what you want

Table 5: Stability prediction parameters: How well they perform in the real world?

Moderator: Shrikant Deshpande, Ph.D., Medarex Inc, a subsidiary of Bristol-Myers Squibb

  • How can we predict the stability of the antibodies in the real world based on early screening techniques such as DSC, aggregation propensity
  • Acclerated deamidation studies: How well they correlate with the in vivo situation?

Table 18: Relationship between Thermal Stability and Expression Level

Moderator: Guna Kannan, Ph.D., Principal Scientist, Protein Science, Amgen


Table 19:  Applying Automation to MAb Screening

Moderator: Le-Ann Hwang, Ph.D., Principal Coordinator / Head, Monoclonal Antibody Unit, Institute of Molecular and Cell Biology-Singapore


Table 20:  Engineering Single-Chain Antibodies for Improved Stability

Moderator: Rosemarie Wilton, Ph.D., Biosciences, Argonne National Laboratory


4:50 Networking Cocktail Reception in the Exhibit Hall

6:00 End of Day

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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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