PEGS Europe 2010 | Day 1  |  Day 2 

A conference that examines this promising new generation of biotherapeutic from cell line selection to creation of libraries, screening and beyond. Industry and academic experts present antigen-binding, potency and ability to reach difficult targets together with in vitro and in vivo pre-clinical investigations and, in some cases, regulatory approval and further clinical study. Characterization and imaging of target binding are included as well as key features such as stability, half-life, and resistance to aggregation and post-translational modification, and application to specialized delivery.


9:00 Conference Registration and Morning Coffee


Engineering the Fc Regions for Antigen Binding,
Effector Function and Enhanced Half-Life

9:30 Chairperson’s Opening Remarks

Christian Heinis, Ph.D.,Laboratory of Therapeutic Proteins and Peptides, Institute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne (EPFL)

9:35 Modular Antibodies: Introducing Antigen-Binding Sites in the Fc Region of IgG

Max WoisetschlagerrMax Woisetschläger, Ph.D., Director, Target Biology, f-star Biography 

We have developed two novel antibody formats: Fcabs, in which antigen-binding sites are introduced into a human Fc fragment; and mAb2s, in which additional binding sites are engineered into the Fc of an intact antibody. Fcabs allow small therapeutic antibody fragments to be isolated that retain all normal antibody functionalities (antigen binding, effector functions and long half life) while mAb2s represents an elegant way to create bispecific antibodies. Examples will be described demonstrating the potential of these proteins as next generation therapeutic biologicals.

10:05 IL-17 Neutralizing Fynomers: Making Use of Fc Fusion Proteins

Dragan GrabulovskiDragan Grabulovski, Ph.D., Chief Scientific Officer, Covagen, A.G. Biography

We describe the design, construction, characterization, and use of a large human Fyn SH3 library comprising 8.5 x 10e10 individual clones (termed Fynomers). The versatility and broad applicability of the Fynomer technology will be presented as well as the in vitro and in vivo characterization of high-affinity Fynomers binding to IL-17. We will demonstrate how engineered Fynomer-Fc fusion proteins having appropriate physico-chemical and in vivo half-life properties are attractive drug candidates for pre-clinical and clinical development.

Sponsored by
10:35 Coffee Break


Novel Delivery Products

11:00 Exploiting the Biophysical Properties of Centyrins for Alternative Routes of Delivery

Steve Jacobs, Ph.D. Principal Scientist, Centyrex Venture, Johnson & Johnson, Inc. Biography 

Alternative scaffolds represent an emerging of protein drugs that combine the attractive specificity properties of mAbs with the simplicity, ease of manufacture and tissue penetration associated with small molecules. We are exploiting the properties of an exceptionally stable alternative scaffold to develop a series of molecules tailored for alternative routes of delivery. The development and application of the Centyrin technology will be presented, together with in vitro and in vivo characterization of high-affinity Centyrins against an array of therapeutic targets.

11:30 Anticalins: A Differentiated Biologics Drug for Novel Delivery, Broad Target Space and New Modes of Action

Kristian JensenKristian H. Jensen, Ph.D., Chief Operating Officer, Pieris AG Biography

Anticalins are modified versions of human lipocalins. Pieris’ lead project PRS-050 (VEGF antagonist) is now entering human studies. Unique features of this drug such as the ability to bind therapeutically relevant hapten targets will be presented with their broad formulation and delivery options and formatting flexibility.

Sponsored by
12:00 Glycan-Binding Decoy Proteins with Strong Anti-Inflammatory Activity Derived from the CellJammer® Platform Technology
Andreas Kungl, CSO, ProtAffin Biotechnologie AG
ProtAffin is developing novel biopharmaceuticals targeting protein-glycan interactions in inflammation. The importance of especially glycosaminoglycans in regulating protein function has been under-exploited as a basis of therapeutics for a long time mainly due to the complexity of this glycan class which prevents easy chemical synthesis. ProtAffin’s CellJammer® discovery platform takes advantage of a protein’s natural glycan-binding function to improve it thereby generating unique decoy proteins with anti-inflammatory, anti-metastatic or anti-angiogenic activity.

12:30 Lunch for Purchase in the Exhibit Hall

13:45 Dedicated Poster Viewing in the Exhibit Hall

Technologies that Select for Enhanced Half-Life
and Stability

14:30 Chairperson’s Remarks

Josefin-Beate Holz, Chief Medical Officer, Ablynx NV

14:35 From Clinical Imaging to Serum Half-Life Extension Using HER2-Specific Affibody Molecules

Fredrik FrejdFredrik Y. Frejd, Ph.D., Project Manager, Biotherapeutics, Affibody AB Biography

Affibody molecules are 6.5-7 kDa scaffold proteins with rapid in vivo kinetics. Pre-clinical data leading to clinical trial regulatory approval for a HER2-targeting Affibody imaging agent will be presented. The half life and distribution profile of the imaging molecule was enhanced using albumin binding technology, allowing for successful targeted radionuclide therapy in xenografted mice. Furthermore, the albumin binding technology is general, as shown in a pharmacodynamic study in rats using modified G-CSF associating with albumin.

15:05 PASylation: A Superior Technology to Extend the Plasma Half-Life of Therapeutic Proteins

Arne SkerraArne Skerra, Ph.D., CEO, XL-protein GmbH Biography

PAS sequences form conformationally disordered biological polymers with large hydrodynamic volume and high solubility, similar to PEG. In contrast, PASylated biopharmaceuticals can be directly produced in microbial expression systems with a wide range of therapeutic proteins, thus avoiding costly and laborious chemical modification steps. PAS sequences can prolong the pharmacokinetics of biologics in mice by a factor of 10-100. Preclinical data for several pharmaceutically attractive protein drug classes, including antibody fragments and alternative scaffolds, will be presented.

Sponsored by
15:35 Refreshment Break



Focus on Screening and Selection of
Drug Candidates for Specific Purposes

16:00 Sponsored Presentation (Opportunity Available)

16:30 Tn3: A New Platform for Non-antibody Protein Drugs

Manuel BacaManuel Baca, Ph.D., Principal Scientist, Antibody Discovery and Protein Engineering, MedImmune, Inc. Biography

We have developed an alternate scaffold platform from a small Ig-like protein module. This scaffold can be expressed at high levels in bacteria and has been engineered for high stability. Sequence and length diversification of surface loops has been used to create large diversity libraries from which target binders can be readily selected. This presentation will describe the unique features of this platform and its flexibility in engineering format and valency for next generation therapeutics.

17:00 Generating A Best-in-Class DARPin Therapeutic for the Treatment of Ophthalmic Neovascularization Diseases

Kaspar BinzH. Kaspar Binz, Ph.D., Vice President Technology, Molecular Partners AG Biography

DARPins combine the advantages of antibodies with those of small molecule drugs and allow us to generate a broad pipeline of innovative new drug candidates in a short time. We will present hands-on data on how we choose the best of the many drug candidates and how we assay them in vitro and in vivo. This process will be illustrated by the example of a best-in-class therapeutic DARPin for the treatment of wet AMD and other ocular neovascularization diseases.

17:30 Challenges in Domain Antibody Development

Thomas Sandal, Head, Microbial Process Research, GlaxoSmithKline Research & Development Biography

GSK has developed an innovative approach for assessing the development of potential novel domain antibodies (dAbs). The strategy comprises high-throughput and downscaled methods to evaluate the biophysical properties and purification challenges for a range of dAbs. In order to develop a commercially viable expression system, a high-throughput method has been implemented to screen a combination of recombinant vector designs and host strains. This high-throughput screening technique facilitates the selection of a production strain and vector based on the productivity and quality
of dAb.

18:15 Interactive Breakout Discussion Groups

19:15 – 21:00 CHI Networking Reception

Sponsored by




Precision Antibody


VTU Technology GmbH