Track 1

As China joins the global biopharm industry in the development of novel biologics, they have to overcome many hurdles in their quest to create the next generation of innovative products. These challenges range from identifying new and emerging targets, improving antibody discovery and library generation, developing rational engineering strategies and designing and optimizing new molecules with the desired properties. At the Protein & Antibody Engineering meeting, we invite researchers to share their passion in the design and optimization of protein and antibody molecules, and to discuss the cutting-edge technologies and creative approaches they used to overcome the challenges along the way.


7:30 am Registration and Morning Coffee


8:50 Chairperson’s Opening Remarks

Mitchell Ho, Ph.D., Chief, Antibody Therapy Section, National Cancer Institute, NIH

9:00 Improved Methods for Designing and Evolving Antibodies

Tessier PeterPeter M. Tessier, Ph.D., Richard Baruch M.D. Career Development Associate Professor, Chemical & Biological Engineering, Rensselaer Polytechnic Institute

The biotech industry has seen an explosion in the development of therapeutic antibodies in the last decade. The advantages of antibodies are compelling. Nevertheless, there are many challenges associated with antibody selection and engineering that require key technical advances to simplify the rapid and reliable generation of potent antibody therapeutics. I will discuss our progress in addressing some of these challenges, including the design, evolution and selection of antibodies with high affinity, stability and solubility.

9:30 Engineering Principles to Generate Multivalent Antibody-TRAIL Fusion Proteins

Roland KontermannRoland Kontermann, Ph.D., Professor, Biomedical Engineering, Institute of Cell Biology and Immunology, University of Stuttgart

Fusion of TRAIL to antibody fragments has been shown to allow for a targeted delivery and the selective induction of tumor cell death. We have engineered optimized single-chain derivatives of TRAIL (scTRAIL), which were employed to develop novel multivalent antibody-scTRAIL fusion proteins with improved properties. These multivalent fusion proteins were generated employing either scFv-driven homodimerization or various separate homodimerization modules. Targeting and controlled dimerization of scTRAIL fusion proteins provides a strategy to enforce apoptosis induction, together with retained tumor selectivity and good in vivo tolerance.

10:00 Coffee Break

10:30 Chairperson’s Remarks

Mitchell Ho, Ph.D., Chief, Antibody Therapy Section, National Cancer Institute, NIH


10:35 Design Principles for Bispecific IgGs – Opportunities and Pitfalls of Artificial Disulfide Bonds

Itai Benhar, Ph.D., Professor, Molecular Microbiology and Biotechnology, Tel-Aviv University

We present a solution for correct pairing of heavy and light chains of bispecific IgGs, an engineered disulfide bond between the antibodies’ variable domains that asymmetrically replaces the natural disulfide bond between CH1 and CL. Bispecific IgGs where the artificial disulfide bond is placed in the CH1-CL interface are also discussed. Examples will be provided for some of these bsAbs and future directions of the study will be discussed.

11:05 Therapeutic Enzymes for the Treatment of Leukemia: Molecular Engineering and in vitro Evolution of L-Asparaginases

Manfred Konrad, Ph.D., Research Director, Enzyme Biochemistry, Max Planck Institute for Biophysical Chemistry

L-asparaginases (L-ASNase) of bacterial origin are FDA-approved enzyme drugs for the treatment of acute lymphoblastic leukemia, despite eliciting adverse side effects, in particular immunogenicity. This talk highlights the rational design and molecular engineering of human homologues to replace bacterial enzymes. We developed a high-throughput screening platform to identify enzyme variants displaying improved catalytic activities, and packaged L-ASNases into microcapsules to enhance protein stability and prevent exposure to the immune system.

11:35 Expression, Structural and Functional Studies of the Human Cannabinoid Receptor CB2

Alexei Yeliseev, Ph.D., Staff Scientist, Group Leader, LMBB, NIH/ NIAAA

Human cannabinoid receptor CB2 is an important target for pharmaceutical drug development. High resolution structural studies are necessary for rational design of specific ligands targeting this receptor. Furthermore, CB2 was site-specifically labeled by selectively targeting reactive cysteine residues and incorporation of unnatural functional groups through codon reassignment which allows preparation of receptor samples for various spectroscopic studies. Studies of the structural dynamics of CB2 bound to a variety of cannabinoid ligands, in detergent micelles and in lipid bilayers of various compositions are in progress.

12:05 pm Sponsored Presentation (Opportunity Available)

12:35 Networking Luncheon in the Exhibit Hall with Poster Viewing

1:55 Chairperson’s Remarks

Yu Zhou, Ph.D., Associate Adjunct Professor, Anesthesia, University of California, San Francisco


2:00 Glycooptimization of Antibodies Results in Improved Clinical Efficiency

Lars Stoeckl, Ph.D., Associate Director, R&D, Glycotope GmbH

Glycosylation is one of the major post-translational modifications of biotherapeutics that depends on the cell line used for production. We have generated a set of glyco engineered human cell lines for the high yield production of fully human glycooptimized antibodies. Two Biobetter antibodies directed against approved targets and glycooptimized with respect to manifold improvement of anti-cancer activity, half-life elongation, removal of immunogenic components are in clinical development. Case studies including results from clinical Phase I studies will be presented.

2:30 Rational Strategy to Stabilize Early Stage Biologic Candidates to Enhance Developability and Enable Successful Transfer from Research into Development

Danny K. Chou, PharmD., Ph.D., President, Compassion BioSolution

The goal of this presentation is to describe a platform approach to identifying the optimal solution conditions that can stabilize biologics candidates in the discovery/candidate selection stage in a high throughput fashion, whereby, using a very limited amount of protein and commonly available equipment, the development team can assist the drug discovery team in candidate selection and re-engineering of molecules prior to transition into full-scale development.

3:00 Viscosity Modulation of Antibodies by Design

Satish D. Singh, Ph.D., Research Advisor, Biotherapeutics Pharmaceutical Sciences, Pfizer, Inc.

Proactively eliminating or mitigating development challenges can reduce the time and resources required for taking a molecule from discovery to clinic. A common development challenge for mAbs is high viscosity of their concentrated solutions. Viscosity in solution depends on intermolecular (self-) interactions, which are determined by the sequence and structural properties. Understanding the molecular origins of these interactions can help to select or design mAb candidates with low viscosity.

3:30 Sponsored Presentation (Opportunity Available)

4:00 Refreshment Break in the Exhibit Hall with Poster Viewing


4:40 Gypican-3 as a Liver Cancer Target for Antibody-Based Therapies

Mitchell Ho, Ph.D., Chief, Antibody Therapy Section, National Cancer Institute, NIH

Glypican-3 (GPC3) is expressed in hepatocellular carcinoma. Our lab has developed human monoclonal antibodies therapeutically targeting GPC3 that inhibit Wnt/Yap signaling pathways known to be important for liver cancer pathogenesis. Furthermore, we have demonstrated that a GPC3-targeted immunotoxin can cause regression of human liver cancer xenografts in mice. Its mechanism of action appears to involve both inhibition of cancer signaling (Wnt/Yap) and reduction in protein synthesis.

5:10 Targeting the Intracellular Proteome with Antibodies against Peptide/MHC Complexes Presented on the Cell Surface: Making the Intracellular Targets Visible to Antibody Therapy

Yoram Reiter, Ph.D., Professor and Head, Molecular Immunology, Biology, Technion-Israel Institute of Technology

The ability to generate T-cell receptor-like (TCRL) antibodies which bind HLA-peptide complexes on the surface of cells opens new possibilities for developing new therapeutic modalities. These antibodies can bind specifically to, and kill, the diseased cells, transforming disease-specific targets expressed inside malignant cells into targets that can be recognized on the cell surface by soluble TCRL antibodies. This approach expands the pool of novel therapeutic antibodies beyond the limits of currently available antibodies.

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

6:40 Close of Day


8:30 am Registration and Morning Coffee

8:50 Chairperson’s Opening Remarks

Herren Wu, Ph.D., CTO, MedImmune/AstraZeneca



Bradbury AndrewAndrew Bradbury, MBBS, Ph.D., Research Scientist and Group Leader, Biosciences Division, Los Alamos National Laboratory

Researchers all over the world routinely use antibodies, a critical class of commercially supplied reagents that are frequently unreliable. This situation affects reproducibility in biomedical research, wastes millions of dollars annually, and may affect clinical trials. This talk will provide an overview of the problem, argue that the time has come to express antibodies recombinantly and refer to them by their sequences, and provide possible ways to get to this ideal.

9:30 Therapeutic Antibody Discovery Using Multiple Tools

Yan Wu, Ph.D., Associate Director and Principal Scientist, Department of Antibody Engineering, Genentech, Inc.

10:00 Sponsored Presentation (Opportunity Available)

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

11:10 Antibody Isotopes Diversity and Their Biomedical Potentials

Xiaoying Zhang, Ph.D., Professor, College of Veterinary Medicine, Northwest A&F University

Antibodies from different species (eg.: IgY, VHH, Bovine IgG, rabbit IgG, Lamprey—VLR) have different biological characters, and these may lead to special medicinal values. It is necessary to study, understand and utilize the antibodies from different species based on their unique advantages/characteristics. Such knowledge is becoming important source for antibody design, antibody engineering and antibody mimics.

11:40 Nature-Inspired Synthetic Human Ab Library

Yu Zhou, Ph.D., Associate Adjunct Professor, Anesthesia, University of California, San Francisco

Naïve human antibody CDR sequences were collated and used to design non-redundant synthetic CDRs matching the naturally occurring diversities. These synthetic non-redundant CDRs were inserted into the well expressing V-gene frameworks, and displayed to construct phage Ab library. Such phage Ab library was used to isolate high quality renewable antibodies (rAbs), which are essential reagents for determining how proteins function under normal and pathophysiological conditions.

12:10 pm Antibody Library Display on a Mammalian Virus: Combining the Advantages of Panning and Cell Sorting in One Technology

Ernest S. Smith, Ph.D., Senior Vice President, Research & CSO, Vaccinex, Inc.

We have developed a new antibody selection technology that enables efficient expression of a library of human antibodies in full length IgG format on the surface of vaccinia virus, an enveloped mammalian virus. Various panning and magnetic bead based methods have been developed to screen the library of vaccinia-MAb virions and select recombinant vaccinia virus encoding specific antibodies. This technology ensures the selected antibodies are efficiently expressed and have favorable stability and specificity properties.

12:40 Networking Luncheon in the Exhibit Hall with Poster Viewing

2:00 Close of Protein & Antibody Engineering

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Track 1

Protein & Antibody Engineering

Track 2

Analytical Characterization of Biotherapeutics

Track 3

Next-Generation Cancer Biotherapeutics

Track 4

Protein Aggregation & Stability


Clinical and Regulatory Strategies for Domestic and Global IND And BLA Filings