January 13 - 17, 2014
Renaissance Hotel and Palm Springs Convention Center Palm Springs, California

A Community Dedicated to the
Evolving Field and Future of Biotherapeutics

Recombinant Protein Therapeutics header

Day 1 | Day 2 | Download Brochure 

Conference Short Courses*View Details 

Sunday, January 9 - 3:00 pm - 6:00 pm

  • Protein Crystallization - Delineating Protein Structure

Thursday, January 13 - 6:30 pm - 9:00 pm

  • Rational Design of Protein Solutions

 

This meeting addresses the innovative strategies and supporting technologies that spur progress, including engineering the Fc regions.  Persistent challenges will be discussed, along with case studies of recombinant protein therapeutic products. In addition, the meeting will explore the different classes of therapeutic fusion proteins currently in development.

MONDAY, JANUARY 10


7:30am  Conference Registration and Morning Coffee

 

Innovating to Overcome Challenges

8:30  Chairperson’s Opening Remarks

Rose E. Sekulovich, Ph.D., Director, Analytical Development, Althea Technologies, Inc.

 

Opening Keynote Presentation

8:45  Protein Therapeutics: Triumphs and Challenges

Lynne ReganLynne Regan, Ph.D., Professor, Molecular Biophysics & Biochemistry, Yale University

To harness proteins’ capabilities for therapeutic applications, one must either co-opt a natural protein or employ design or selection approaches to create new proteins with the desired activity. One must also ensure that the desired protein therapeutic has suitable pharmokinetic properties. I will discuss examples of disease in which the molecular basis is well suited to correction by protein-based therapeutics. I will also compare and contrast different approaches to creating proteins for therapeutic applications, highlighting both successful examples and ongoing challenges.



Featured Presentation

9:35  Recombinant Proteins for Targeting Intracellular Compartments of Cancer Cells

Debinski WaldemarWaldemar Debinski, M.D., Ph.D., Director, Brain Tumor Center of Excellence; Head, Section of Tumor Biology, Department of Neurosurgery; Professor of Neurosurgery, Radiation Oncology and Cancer Biology, Wake Forest University Health Sciences, Wake Forest Comprehensive Cancer Center

Most anti-cancer therapeutics have defined targets such as oncogenes, enzymes or DNA, all of which are localized to distinct intracellular compartments like cytosol, mitochondria or nuclei. We reasoned that having direct delivery vectors for therapeutics/labels to these subcellular compartments will lead to an increased specificity, efficacy and less toxicity. To this end, we designed a multiple-specificity delivery vehicle targeting the Interleukin 13 Receptor alpha 2 (IL-13Rα2) for efficient transport to the nuclei of Glioblastoma multiforme (GBM) cells. We have demonstrated in a direct way that molecularly targeted, genetically engineered single-chain protein specifically recognizes GBM cancer cells, travels to and accumulates in these cells’ nuclei.


10:05  Networking Coffee Break

 

Case Studies

10:45  ACE2: From Concept to the Patient

Manfred Schuster, Ph.D., COO, Apeiron Biologics AG

We are developing a soluble form of recombinant human Angiotensin Converting Enzyme 2 (rhACE2) for systemic treatment of various conditions. This talk will give an insight into the first administration of rhACE2 to humans focusing on its pharmacologics properties. As a next step, a Phase II clinical trial in Acute Respiratory Distress Syndrome is in preparation and will be conducted by our partner GlaxoSmithKline.

11:15  Therapeutic Assessment of SEED: a New Protein Platform for Mono and Multifunctional Antibodies

Alec W. Gross, Ph.D., Principal Investigator, Protein Engineering and Antibody Technologies, EMD Serono Research Institute, Inc.

Engineered antibody and antibody-like proteins are the emerging “State of the Art” for the Next Generation of Biologics. We will present the development of a heterodimer protein scaffold with critical antibody-like properties and with the added potential of efficiently generating multifunctional therapeutics by fusion with a variety of protein domains. This heterodimeric protein platform has potential to open new opportunities through new mechanisms of action, increased specificity and delivering combination therapy in one molecule.

11:45  Recombinant Factor IX Monomeric Fc Fusion Protein (rFIXFc): Concept to Clinic

Alan J. Bitonti, Ph.D., Senior Vice President, R&D, Biogen Idec

Fusion of various effector molecules to the Fc domain of immunoglobulin G has been a successful approach for extending their biological half-life. However, certain therapeutic proteins, e.g. blood coagulation factors, were difficult or impossible to manufacture as traditional dimeric Fc fusion proteins. To address this problem we created a proprietary of monomeric Fc fusion proteins comprised of a single effector molecule attached to the Fc domain of IgG1. In addition, to improve manufacturability, monomeric Fc fusion proteins have enhanced biological activities. One of these novel molecules, rFIXFc, is currently in late-stage clinical trials.

12:15pm  Close of Morning Session

12:30 Luncheon Presentations (Sponsorship Opportunities Available) or
Lunch on Your Own

 

Optimizing Properties

2:00  Chairperson’s Remarks

Waldemar Debinski, M.D., Ph.D., Director, Brain Tumor Center of Excellence; Head, Section of Tumor Biology, Department of Neurosurgery; Professor of Neurosurgery, Radiation Oncology and Cancer Biology, Wake Forest University Health Sciences, Wake Forest Comprehensive Cancer Center

2:05  Disulfide Linkages of an Albumin Fusion Protein

Andréa Meeler, M.S., Research Associate, Analytical Sciences:  Biochemical Characterization, Human Genome Sciences, Inc.

Accurately determining the connectivity of disulfide bonds is important for therapeutic recombinant proteins, as disulfide bonding contributes to overall protein structure and function.  Disulfide bonds can be assessed by a variety of methods, however, when cysteine residues are adjacent in the protein sequence, disulfide linkage analysis becomes a challenge.  We used LC-MS, MALDI-Tof MS, partial reduction, and a novel approach using Edman sequencing to verify the linkages in an albumin-fusion protein, where the majority of disulfide bonds involve adjacent cysteine residues.

2:35  In vitro Characterization of an Acetylcholine Receptor-Transferrin Fusion Protein

Serene Josiah, Ph.D., Director, Discovery Research, Shire Human Genetic Therapies

Myasthenia gravis (MG) is an autoimmune disease caused predominately by alpha subunit autoantibodies. SHG2210, a fusion protein containing the N-terminus of human AchR-α (nicotinic acetylcholine receptor α; aa1-210) and human transferrin (TF), was characterized in vitro as a potential therapeutic.  SHG2210 binds to alpha subunit autoantibodies and the TF receptor and the SHG2210/anti-AchR antibody complex is internalized through transferrin receptor-mediated endocytosis. SHG2210 is shown to have a protective effect on antigenic modulation of the AChR induced by serum from select patients with MG.

3:05  Biopolymer ELP-Fusion Protein Technology Significantly Enhances the Pharmacology, Safety, and Efficacy of Biotherapeutics

Lynne M. Georgopoulos, RN, BS, RAC, Senior Vice President Clinical Development, PhaseBio Pharmaceuticals, Inc.

Polymers of varying length and amino acid composition at the X position are fused to therapeutically active peptides and proteins. ELPylated proteins have the following common attributes ideal for clinical development: high potency, peakless (no burst) subcutaneous delivery with sustained release-like kinetics. The result is products with improved tolerability and efficacy. These attributes allow delivery of protein therapeutics with sustained exposure in the targeted therapeutic range with once-weekly to once-monthly dosing using a simple pen device.

3:35  Sponsored Presentation (Opportunity Available)

3:50  Networking Refreshment Break

 

Designing Fusion Proteins to Fight Disease

4:30  Recombinant Transferrin Fusion Proteins for the Activation of Protein Precursors in Liver: The Conversion of Proinsulin to Insulin as a Transferrin Fusion Protein in Hepatoma Cells

Wei-Chiang Shen, Ph.D., John A. Biles Professor, Pharmacology & Pharmaceutical Sciences, University of Southern California School of Pharmacy

A full-length proinsulin-transferrin (ProINS-Tf) recombinant fusion protein was produced from transfected HEK293 cells. ProINS-Tf exhibited delayed but enhanced insulin activities in H4IIE hepatoma cells, including the activation of downstream insulin receptor signaling and the inhibition of gluconeogenesis. These increased activities were significantly inhibited by the co-incubation with excess transferrin (Tf), indicating that the increased activity of ProINS was facilitated through Tf receptor (TfR)-mediated endocytosis. These findings reveal the potential applications in using recombinant fusion technology for the design of protein prodrugs to be activated in the liver.  

5:00  Small and Simple Cysteine-Containing Fusion Tag for Site-Specific Payload Conjugation

Joseph M. Backer, Ph.D., CEO, SibTech, Inc.

For clinical development, site-specific conjugation of therapeutic and imaging payloads to targeting proteins is highly advantageous. To simplify and standardize site-specific conjugation, we have recently developed a 15-aa humanized cysteine-containing fusion tag (Cys-tag), which proved to be compatible with a variety of targeting proteins and payloads of resulting therapeutic and imaging agents. Several agents based on Cys-tagged proteins are in late pre-clinical development. From fluorescent dyes to ultrasound microbubbles, coupling of payloads did not affect either binding or internalization.

5:30  SCORPION Therapeutics: Multi-Specific Proteins with Enhanced Biologic Activity

Alan Lofquist, Ph.D., Director, Research, Emergent Product Development Seattle

SCORPION™ proteins are single chain, multi-specific molecules that can neutralize two soluble targets or deliver tolerogenic cytokines (e.g., IL-10) to antigen-presenting cells. Scorpion proteins can utilize scFv’s, receptor ectodomains or cytokines as active biologic components. In comparison to mono-specific proteins, the SCORPION™ molecules have demonstrated enhanced activity both in vitro and in vivo.

6:00  Welcoming Reception in the Exhibit Hall

7:30  Close of Day

 

Day 1 | Day 2 | Download Brochure 



Links to Companion Meetings

Pipeline 1

Antibodies for the 21st Century 

Antibody Drug Products


Japan-Flag Korea-Flag China-Simplified-Flag China-Traditional-Flag 


PTK Event APP 
New this year!
The PepTalk App will allow attendees to browse the agenda, create custom schedules, navigate the exhibit hall and explore poster presentations.

2014 Brochure Cover 

Right Arrow Download the Brochure 

Right Arrow Event at-a Glance 

      Premier Sponsors: 

EMD Millipore 

 Novozymes (white) 

PerkinElmer NEW 2009 

 Protein Simple  

  

Right Arrow View All Sponsors 

Right Arrow View Media Partners 

Add to Outlook Add to Outlook 

Training Seminars 

Mon-Tues, January 13-14 

Biologics Formulation and Delivery  

 


Buzz Sessions
BuzZ Sessions are facilitated, small-group discussions. Interactive participation leads to problem-solving solutions and future collaborations around focused topics.
Click here for BuzZ topics