Cambridge Healthtech Institute’s 2nd Annual 

Protein & Antibody Engineering 
蛋白质和抗体工程
Innovative Engineering * Novel Scaffolds * Bispecific Antibodies

March 31-April 1, 2015

 

The field of protein engineering is at an exciting point in its development, with new generations of protein and antibody formats entering the market, improved understanding of structure-function relationships, and creative engineering that promises to optimize molecules with improved biophysical properties.

The Protein & Antibody Engineering conference presents the state of the art in strategies and techniques to enhance antibody binding and specificity, design of novel scaffolds with increased potency, as well as new and enhanced applications for bispecific antibodies.


Thursday, March 31


Day 1 | Day 2 | Download Brochure 

7:30 am Registration and Morning Coffee

8:50 Chairperson’s Opening Remarks

Dimiter Dimitrov, Ph.D., Senior Investigator, NCI, National Institutes of Health


ENHANCING ANTIBODY BINDING, SPECIFICITY AND
DRUG-LIKE PROPERTIES

9:00 Antibody Engineering for Better in vivo Efficacy

Weidong Jiang, Ph.D., CSO, Henlius Biopharmaceuticals, Inc.

Antibody engineering is a great tool for improving antibody functions in vivo. We have routinely engineered therapeutic antibodies for better in vivo efficacies via affinity maturation, specifically by improving on-rate of the antibody binding affinities. One particular case will be reported here for better functions in vivo as well as other functions such as immunogenicity improvement.

9:30 In vitro and in vivo Study of pH-Dependent Antigen Binding Antibody with Increased FcgammaRIIB Binding

Yuji Hori, Ph.D., Research Scientist, Chugai Pharmaceutical, Japan

Sweeping antibody with enhanced FcR mediated cellular uptake of antibody-antigen complex and pH-dependent endosomal antigen dissociation enables antigen elimination from plasma, providing enhanced efficacy and novel mode of action for antibody therapeutics. This talk will present an in vivo profile of sweeping antibody and its in vitro confocal microscopic study to address the intracellular trafficking of the soluble antigen.

10:00 Design and Develop Next-Generation Bispecific Antibodies with Good Drug Like Properties (DLP)

Jinming Gu, Ph.D., Senior Scientist, Global Biologics, Abbvie, Inc.

Bispecific antibodies have emerged as the next generation of antibody-based therapeutics. So far, there have been more than 50 different bispecific antibody platforms published in the literature. However, it continues to be a major challenge to identify bispecific antibodies with good drug like properties which functions preclinically. This presentation will discuss different approaches we are utilizing to design and develop bispecific antibodies with good drug like properties.

10:30 Coffee Break


NOVEL PROTEINS AND ALTERNATIVE SCAFFOLDS

11:00 Anticalins: Versatile Binding Proteins based on a Flexible Natural Scaffold

Arne Skerra, Ph.D., Professor, Technische Universität München; Founder, Pieris AG, Germany

Anticalins are derived from human lipocalins, whose four structurally hypervariable loops form a binding site that can be tailored against medically relevant targets. However, anticalins are much smaller and comprise a single polypeptide chain, offering facile production in microbial hosts and flexible formatting: multiple specificities, attachment of payloads and extended plasma half-life via PEGylation or PASylation. Two anticalins have reached clinical stage for therapeutic applications.

11:30 ADAPT - A Novel Scaffold Protein for Radionuclide Molecular Imaging

Johan Nilvebrant, Ph.D., Postdoctoral Researcher, The Donnelly Centre, Center for Cellular and Biomolecular Research, University of Toronto, Canada

ADAPTs (ABD-derived affinity proteins) are a novel class of scaffold-based affinity proteins, which are derived from the albumin-binding domain (ABD) of streptococcal protein G. They have been generated in a bispecific format to target various antigens. These radiolabeled ADAPTs were recently used to provide high contrast PET-images of HER2 positive tumor xenografts shortly after injection and show promise as a new class of imaging agents.

12:00 pm Sponsored Presentation (Opportunity Available)

12:30 Networking Luncheon

1:45 Chairperson’s Remarks

Dimiter Dimitrov, Ph.D., Senior Investigator, NCI, National Institutes of Health


NOVEL PROTEINS AND ALTERNATIVE SCAFFOLDS (cont’d)

1:50 Exceptionally Potent and Broad Inhibitors of HIV-1 based on Antibody Domains and One Domain Soluble CD4 Multivalent Fusion Proteins

Dimiter Dimitrov, Ph.D., Senior Investigator, NCI, National Institutes of Health

We generated bispecific multivalent fusion proteins of an engineered cavity-altered single-domain CD4 with another potent HIV-1 inhibitor - an antibody domain targeting the coreceptor-binding site on gp120. The fusion proteins neutralized all HIV-1 isolates tested with potency about 10-, 50-, and 200-fold higher than that of VRC01, T20, and sCD4-Fc fusion protein CD4-Ig, respectively. These fusion proteins could be potentially useful for HIV-1 therapy including eradication of the virus.

2:20 Cross-Neutralizing Single-Domain Antibodies to Pandemic Influenza

Simon E. Hufton, Ph.D., Principal Scientist, Biotherapeutics, National Institute for Biological Standards and Control (NIBSC)

The response to the 2009 A(H1N1) influenza pandemic has highlighted the need for additional strategies for intervention which preclude the prior availability of the influenza strain. We have isolated single domain antibodies with broad neutralisation activity from immunised alpaca’s and used yeast display technology to investigate antibody/antigen interactions to assist in the understanding of their mechanism of action. These single domain antibodies are attractive candidates for diagnostics and immunotherapy of pandemic influenza.

2:50 Meditopes: Development of Noncovalent Peptide-Fab Interaction to Rapidly and Specifically Add Functionality to mAbs

John C. Williams, Ph.D., Associate Professor, Molecular Medicine, Beckman Research Institute at City of Hope

MAbs require chemical conjugation and/or extensive re-engineering to deliver toxins, imaging agents and other functionalities to diseased tissues. Herein, we present the discovery of a novel cyclic peptide (aka a meditope) that binds to the cavity of cetuximab Fab. While this binding site is unique to cetuximab, it can be grafted on to mAbs. Studies will be presented highlighting the rapid and efficient functionalization of mAbs.

3:20 Sponsored Presentation (Opportunity Available)

3:50 Refreshment Break


Plenary Keynote Session

4:35 Keynote Introductions 

Weidong Jiang, Ph.D., CSO, Henlius Biopharmaceuticals, Inc. 

4:40 Antibody Development Strategies in Today’s China 

Chengbin WuChengbin Wu, Ph.D., President, R&D and CSO, Shanghai C.P. Guojian Pharamceutical Co. Ltd., PR China 

In the past 10 years, commercial manufacturing of antibodies at GMP standard has become possible in China, leading to successful commercialization of several antibody-based therapeutics, with many more in various stages of development. This talk will provide a brief overview of antibody development in China, with a case study discussing key aspects of developing an anti-Her2 antibody that has completed Phase III clinical trials in China. 

5:10 Designing and Engineering Novel Bispecific/Bifunctional Antibodies and Fusion Proteins for Enhanced Antitumor Activity 

Zhenping ZhuZhenping Zhu, Ph.D., Executive Vice President, Global Biopharmaceuticals, Kadmon Corporation 

Major obstacles in the successful development of BsAb (bispecific antibodies) have been the difficulties of designing and constructing a druggable molecule and producing sufficient materials for development and commercialization. The technological challenge is to construct a recombinant molecule with good pharmaceutical properties. Developing highly effective BsAb and bifunctional proteins will require clear elucidation and understanding of the molecular details in the aberrant signaling pathways that lead to various diseases to guide the selection of the target pairs for co-targeting. 


5:40 Welcome Reception in the Exhibit Hall with Poster Viewing

6:40 Close of Day

Thursday, March 31


Day 1 | Day 2 | Download Brochure 

8:30 am Registration and Morning Coffee

8:50 Chairperson’s Opening Remarks

Stephen Mahler, Ph.D., Professor, Australian Institute for Bioengineering and Nanotechnology, University of Queensland


NOVEL APPLICATIONS FOR BISPECIFIC ANTIBODIES

9:00 Therapeutic Applications of DART Proteins – What’s Next?

Syd Johnson, Ph.D., Vice President, Antibody Engineering, MacroGenics, Inc.

Bispecific antibodies that recruit effector cells to tumors represent a highly potent class of immunotherapeutic agents that may outperform or complement traditional chemotherapy, naked antibodies and ADCs. MacroGenics’ Dual-Affinity Re-Targeting (DART) proteins are among the most stable and potent biologics in this therapeutic class. This talk will highlight several DART proteins currently in clinical studies and those entering clinical studies, as well as new formats and specificities that are under development for future drug candidates.

9:30 Antibody Engineering Strategies for the Production of Bispecific Heterodimeric IgG in Mammalian Cells

Wei Yan, Ph.D., Director, Research, Therapeutic Discovery, Amgen, Inc.

10:00 Sponsored Presentation (Opportunity Available)

10:30 Coffee Break in the Exhibit Hall with Poster Viewing

11:10 Clinical Development of Tanibirumab and Its Bispecific Antibody, DIG-KT

Jin-San Yoo, Ph.D., President & CEO, PharmAbcine, Inc., Korea

Tanibirumab has completed a Phase I study. In contrast to other KDR pathway antagonists, Tanibirumab did not cause hypertension and hemorrhage side effects, and due to its cross-species cross reactivity, it has been possible to assess in in vivo efficacy studies. I’ll discuss Tanibirumab’s Phase I&II GBM trials, and development of bispecific next-generation products to enable Tanibirumab to reach its full potential.

11:40 Bispecific Antibody Formats Tailored for Specific Applications

Jochen Kruip, Ph.D., Department Head, BioInnovation Novel Therapeutic Protein Formats, Sanofi

Besides a bispecific antibody targeting Il13- and IL4 (currently in phase II) we have further developed our original format to allow specific applications such as T cell engagement.

12:10 pm Targeted Delivery of Nanomedicines Using Bispecific Antibodies

Stephen Mahler, Ph.D., Professor, Australian Institute for Bioengineering and Nanotechnology, University of Queensland

Although there are around 8 nanomedicines approved for cancer therapy, none of these are actively targeted to cancer receptors. Active targeting can increase the proportion of drug payload that reaches the tumour site(s). The utility of targeting nanoparticles to tumour cells with bispecific antibodies (BsAbs) is demonstrated, whereby one arm binds the nanoparticle, and the other the target. The use of BsAbs has several advantages over chemical conjugation of antibody fragments to nanoparticles.

12:40 Networking Luncheon in the Exhibit Hall with Poster Viewing and Close of Protein & Antibody Engineering Conference



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Track 1

Protein Engineering 

Track 2

Phage & Yeast Display 

Track 3

Antibody-Drug Conjugates 

Track 4

Characterization of Biotherapeutics