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Antibodies for the 21st Century

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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.

THURSDAY, JANUARY 13


Sponsored by
Lonza 
7:30am  Breakfast Presentation
De-Risking Your Pipeline: Strategies to Optimize Protein Leads, Reduce Immune Responses and Improve Drug Lead Attrition Rates
Philippe Stas, Ph.D., Head of Applied Protein Services, Lonza
Fredrik Frejd, Ph.D., Project Manager, Biopharmaceuticals, Affibody AB
Development risk and attrition rates remain two of the greatest challenges to a successful biopharmaceutical pipeline. To mitigate risks and improve the chance of success, drug developers need tools that provide a window to a biologic's future -- advanced tools that will help identify potential challenges and improve the quality, safety, efficacy and manufacturability of antibodies, therapeutic proteins, peptides and vaccines.

These presentations will provide a strategic roadmap for optimizing protein leads, reducing immune responses and improving drug lead attrition rates. We will analyze approaches in light of the latest regulatory developments, as well as present selected case studies showing the clinical relevance of the de-risking techniques.

Engineering to Fight Disease

8:15  Chairperson’s Opening Remarks

Christian Heinis, Ph.D., Assistant Professor, Institute of Chemical Sciences and Engineering, EPFL

8:20  Mono- and Multispecific Candidate Therapeutics Based on Engineered Antibody Domains

Dimiter Dimitrov, Ph.D., Head, Protein Interaction Group; Senior Investigator, CCR Nanobiology Program, NCI-Frederick, NIH

Engineered single antibody domains are small and can access targets and epitopes that are not accessible by larger molecules. We have constructed VH- and CH2-based libraries of high diversity from which binders against HIV and cancer-related proteins were identified and characterized with potential use as therapeutics. Multispecific fusion proteins targeting different epitopes on the HIV-1 envelope glycoprotein based on some of the binders were developed that exhibited exceptionally potent and broad inhibitory activity. Further engineering to confer additional functions is in progress.

8:50  Antibody Fusion Proteins for the Treatment of Malignancy

Sherie L. Morrison, Ph.D., Chair, Department of Microbiology, Immunology, & Molecular Genetics, Molecular Biology Institute, University of California, Los Angeles

Type 1 interferons (IFNs) have shown great promise in the treatment of many malignancies, however their use has been limited by their toxicity. We have now produced antibody fusion proteins in which IFN-a or IFN-b are genetically fused to the heavy chain of an antibody recognizing a tumor associated antigen. The fusion proteins retain their ability to recognize the tumor associate antigen and possess IFN activity and have be used to successfully treat established tumors in the absence of systemic toxicity.

9:20  Immunoconjugates for Oncology: Fewer Barriers to Delivering Cytotoxicity Now?

Alejandro D. Ricart, M.D., Director, BioTherapeutics R&D, Pfizer, Inc.

The main objective of immunoconjugate development in oncology is to combine the specificity of immunoglobulins with the efficacy of cytotoxic effector molecules. This therapeutic approach has been validated in hematologic malignancies; however, several obstacles have been identified for achieving efficacy in solid tumors including the inability to optimize structural components, insufficient tumor specificity of target antigens, and poor monoclonal antibody (mAb) delivery, most specifically to the tumor core. However, considerable advances in cancer biology and antibody engineering are contributing to the emergence of efficacious novel agents.

9:50  Best Practices used in the Design of Computer Based Models for AntibodiesSponsored by
Accelrys sm

Francisco G. Hernandez-Guzman, Ph.D., Product Manager Life Sciences, Accelrys, Inc.
Interest in antibody based therapies has seen tremendous growth in pharmaceutical, biotech and academic. These institutions seek to use antibodies as alternative therapeutic agents to classical small molecule therapies. In this presentation, we will explore the process of building a high quality homology model for an Fab domain and we will discuss some of the challenges that one typical encounters during the model building process. We will also emphasize methodologies used to refine the Complimentary Determining Regions of the antibody, and in particularly explore some approaches that can be used to increase the reliability of modeling the challenging H3 loop.

10:05  Coffee Break, Exhibit and Poster Viewing

10:30  Poster Awards in the Exhibit Hall

10:45  Endogenous Anti-IFNa Autoantibodies in Patients with Systemic Lupus Erythematosus are Associated with Decreased IFN-Pathway and Disease Activity

Alyssa Morimoto, Ph.D., Scientist, Bioanalytical R&D, Genentech

Given the proposed central role of IFNa in SLE, therapeutics targeting the type I IFN pathway for the treatment of SLE are in development. The safety, tolerability, and pharmacokinetics of rontalizumab are currently under investigation. Rontalizumab is a humanized IgG1 monoclonal antibody specific for human IFNa. Based on an initial observation that rontalizumab-naïve SLE patient sera exhibited high and variable inter-patient signals in a method developed to detect rontalizumab, we explored whether this activity was due to pre-existing endogenous anti-IFNa autoantibodies in SLE serum.

11:15  Bicyclic Peptides with Antibody-Like Binding Affinity and Specificity

Christian Heinis, Ph.D., Assistant Professor, Institute of Chemical Sciences and Engineering, EPFL

We are generating bicyclic peptide ligands with high affinities and specificities for disease targets using an approach that I had recently developed with Sir Greg Winter at the Laboratory of Molecular Biology (LMB) in Cambridge, UK (1).  Briefly, phage-encoded linear peptides are chemically modified to obtain combinatorial libraries of bicyclic peptides and subjected to affinity selections.  The bicyclic peptides combine key qualities of antibody therapeutics (high affinity and specificity) and advantages of small molecule drugs.

11:45  Extending Half-Life Through Targeted PEGylation

Antony Godwin, Ph.D., Director, Chemistry, PolyTherics Ltd.

PEGylation continues to be a clinically successful solution to half-life extension for new biopharmaceuticals, including antibody fragments.  This talk will focus on the new methods of PEGylation that PolyTherics has developed to improve yield and homogeneity while maximising protein activity, with examples that include antibody fragments and domain antibodies.  By using PEGylation reagents that can specifically target disulfide bonds (TheraPEGTM) and histidine tags (HiPEGTM), it is possible to consider PEGylation earlier in the development process because no additional modifications of the protein are required.

Sponsored by
Selexis
12:15pm  The Role of Technology and 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.

12:45  Luncheon Presentation (Sponsorship Opportunity Available) or Lunch on Your Own

1:30  End of Conference

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Links to Companion Meetings

Pipeline 1

Recombinant Protein Therapeutics 

Antibody Drug Products