8:15 Chairperson�fs Remarks

8:20 Enzymatic Introduction of Thioether Rings in Therapeutic Peptides: Proteolytic Resistance and Enhanced Therapeutic Potential 
Gert Moll, Ph.D., Project Leader, Biomade Technology Foundation
We have demonstrated broad application of lantibiotic enzymes for stabilization of medically and economically highly important therapeutic peptides. We obtained active thioether-ring-containing peptides, which are strongly resistant against proteolytic breakdown in vitro and in vivo. The data indicate strongly enhanced therapeutic potential of the biotechnologically produced thioether-ring-stabilized therapeutic peptides.

8:50 Targeting and Inhibiting Oncogenic Transcription Factors with D- and L-Peptides 
Katja Arndt, Ph.D., Head, Protein Engineering and Signal Transduction Group, Biology, University of Freiburg
Peptides targeting oncogenic transcription factors are of utmost therapeutic interest. We use rational design in combination with in vivo and in vitro selection systems combining competitive and negative design aspects. Peptides specifically directed against the protein-protein interaction domain of such transcription factors were generated. In addition, we compiled a �ebZIP coiled-coil interaction prediction algorithm�f (bCIPA) for the prediction of coiled coil-mediated protein-protein interaction of natural proteins as well as designed inhibitors. Cellular assays demonstrate inhibitory effects of our peptides. To improve the serum half-life time, we also explored D-peptides for targeting oncogenic c-Fos using retro-inverso design as well as mirror-image phage display.

9:20 Phylomers: A New Class of Peptide from Biodiverse Genomes, Suitable for Targeting Intracellular as well as Extracellular Proteins
Paul Watt, D.Phil., Vice President, Drug Discovery, Phylogica Ltd. & Adjunct Associate Professor, University of Western Australia
Proteins such as antibodies can exhibit high specificity, low toxicity and block targets that are difficult to block by conventional means. However, due to their large size and the presence of disulphide bonds, they are not ideally suited to blocking intracellular targets. Peptides can be delivered into cells but often lack biological activity in vivo. Phylomers are a new class of peptide derived from genomic fragments of biodiverse archael and bacterial species. These new peptides may offer major advantages in the ability to access targets such as transcription factors that are challenging to block with small molecules or with larger proteins such as antibodies or protein-based scaffolds. Libraries of Phylomers may also offer greater structural diversity since they represent multiple classes of protein folds.

9:50 Coffee Break in the Exhibit Hall

10:45 RAV12: An Antibody to a Novel Glycotope Present on Adenocarcinomas that Acts Via Oncosis, Receptor Downregulation and Host Effector Function 
Jennie Mather, Ph.D., Founder & Chief Scientific Officer, Raven Biotechnologies
RAV12 is a chimeric antibody that recognizes a novel N-linked carbohydrate antigen (RAAG12) strongly expressed on multiple solid organ cancers. Greater than 90% of tumors of colorectal, gastric, and pancreatic origin express RAAG12. RAV12 exhibits potent cytotoxic activity in vitro against COLO 205 colon tumor cells via an oncotic cell death mechanism. A phase 2 trial in pancreatic carcinoma is expected to begin in Q4, 2007.

11:15 Recombinant Polyclonal Antibody Manufacturing
John Haurum, Chief Scientific Officer, Symphogen A/S, Denmark
Symphogen�Ls Sympress^TM technology enables manufacturing of target-specific recombinant polyclonal antibodies for therapeutic use. The preparation of this new class of drugs is based on a one-pot production strategy starting from a polyclonal cell bank consisting of multiple stable mammalian cell lines each expressing different individual antigen-specific antibodies. Clinical testing with the first drug product prepared by use of Sympress^TM was initiated in 2007. The employed polyclonal cell banking and characterization approach will be discussed.

11:45 Development and Characterization of Novel Dual Affinity Re-Targeting (DART) Molecules 
Syd Johnson, Ph.D., Vice President, Antibody Engineering, MacroGenics, Inc.
A novel format has been developed to create potent and highly stable bispecific molecules (DARTs) for pharmaceutical applications. In particular, DART proteins have been developed that exploit Fc?RIIb, the inhibitory Fc receptor, for indications in oncology and autoimmunity. Studies and properties of DART molecules critical for clinical and product development will be presented, including expression and stability data as well as their in vitro and in vivo activity.

12:15pm Close of Morning Session

2:00 Chairperson�fs Remarks

2:05 Identification, Characterization and Engineering of Novel Human Domain Antibodies Against HIV-1 and Cancer
Dimiter Dimitrov, Ph.D., Senior Investigator, Protein Interactions, CCRNP, CCR, NCI-Frederick, NIH

2:35 Domain Antibody (dAb) Targeting TNF-alpha - From Concept to Clinic
David S. Wilson, Ph.D., Vice President, Antibody Products, Arana Therapeutics
Domain antibodies (dAbs), the smallest functional antigen-binding units, offer potential for enhanced stability, production yields, tissue penetration and formatting flexibility, and reduced immunogenicity compared with full-size antibodies. Combinatorial methods yielded a potent TNF-alpha-neutralizing dAb, which was formatted into a bivalent Fc construct, PN0621, only half the size of an IgG. PN0621 is produced at extremely high yields, is safe and effective in animals and is the first human framework domain antibody to enter the clinic.

3:05 Engineering Multi-Format Bispecific Antibodies via Combinatorics from a Single Human Library 
Robert Mabry, Ph.D., Senior Scientist, Protein Engineering & Antibody Discovery, ZymoGenetics Inc.
Bispecific antibodies (bsAbs) present an attractive approach to combine the additive and potentially synergistic effects of monotherapeutics. One complication in engineering bsAbs is molecule construction with retention of affinity and stability comparable to the parent antibody. Here we present a combinatorial strategy employing shuffling techniques to isolate a variety of antibody formats conducive to bsAbs using a single human phage display library.

3:35 Technology Spotlight 

3:50 Refreshment Break in the Exhibit Hall

4:30 BuzZ Sessions - Small Group Moderated Discussions Have a topic idea?

5:30 Close of Day