Cambridge Healthtech Institute’s Ninth Annual
Protein Purification and Recovery
Streamlining Processes with Innovative Technologies
January 10-11, 2017 | Hilton San Diego Bayfront | San Diego, CA
Protein purification is the most costly and time-consuming process in the manufacture of proteins. Challenges are multiplied when purifying complex molecules, such as membrane proteins, bispecifics or antibody-drug conjugates. This leading purification
meeting on Protein Purification and Recovery will explore how experts are optimizing processes to achieve pure protein while curtailing cost and time. Along with innovating “traditional” technologies such as Protein A and chromatography,
leaders will also address alternatives and breakthroughs, such as continuous processing.
1:00 pm Conference Registration
1:30 Refreshment Break in the Exhibit Hall with Poster Viewing
2:00 Chairperson’s Opening Remarks
William Gillette, Ph.D., Principal Scientist, RAS Protein Production, and Deputy Director, Protein Expression Laboratory, Leidos Biomedical Research, Inc., Frederick National Laboratory for Cancer Research (FNL)
2:05 Advances in Purification Technologies Accelerate Vaccine Development
Yan-ping Yang, Ph.D., Senior Director and Head, Bioprocess R&D North America, Sanofi Pasteur
Over the last 25 years, significant breakthroughs in bioprocesses have been achieved. The advances in downstream technologies have benefited the vaccine industry enormously as purifying vaccine candidates to achieve consistent purity and quality in a
timely manner is an integral part of the vaccine product development process. Case studies will be presented to illustrate how advances in purification technologies have facilitated vaccine process development and moved candidates faster to clinical
2:45 Using Interaction Proteomics to Identify Novel Signaling Components Relevant for Cancer
Alexey Veraksa, Ph.D., Associate Professor, Biology, University of Massachusetts, Boston
We are interested in the structure and function of signaling networks that control cell proliferation and differentiation, and in the mechanisms that cause aberrant signaling through these networks in disease. We interrogate signaling pathways using interaction
proteomics, in particular, affinity purification-mass spectrometry (AP-MS). When applied to cancer-relevant pathways, such as Notch, RTK/ERK, and Hippo, our approaches have identified novel interactions that control these signaling networks under
normal and pathological conditions.
3:15 SELECTED POSTER PRESENTATION
Protein Purification at the CHO Cell Line Engineering and Design Department
Stefan Kol, Ph.D., Protein Biochemist, Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark
3:45 Refreshment Break in the Exhibit Hall with Poster Viewing
4:30 New Chemical Tools for Stabilization of Membrane Proteins
Qinghai Zhang, Ph.D., Associate Professor, Integral Structural and Computational Biology, The Scripps Research
Integral membrane proteins comprise about a third of proteins encoded in genomes and more than half FAD-approved drug targets. The hydrophobic nature of membrane proteins requires their solubilization as isolated stable and functional particles but
also presents a challenge for many biochemical and biophysical studies. We will present new chemical tool development that enhances the stability of membrane proteins and enables successful structural determinations.
5:00 Solving the Challenges of Membrane Proteins through Nanotechnology
Stephen G. Sligar, Ph.D., Director, Swanlund Endowed Chair, Molecular and Cellular Biology, The University
Membrane proteins are involved in numerous vital biological processes, including transport, signal transduction and the enzymes in a variety of metabolic pathways. Unfortunately, membrane proteins are inherently recalcitrant to study using the normal
toolkit available to scientists. The Nanodisc platform circumvents these challenges by providing a self-assembled system that renders typically insoluble, yet biologically and pharmacologically significant, targets such as receptors, transporters,
enzymes, and viral antigens soluble in aqueous media.
5:30 Close of Day
WEDNESDAY, JANUARY 11
8:00 am Conference Registration and Morning Coffee
8:30 Chairperson’s Remarks
Christopher Gray, Ph.D., Structural Biology Team Leader, Drug Discovery Program, CRUK Beatson Institute
8:35 Magnetic Beads for Antibody Purification
Ray Low, Ph.D., Scientist, Biologics Optimization, Amgen
Current linear chromatography technologies take relatively long purification processing time from CM to purified protein. I will talk about how, using the magnetic beads with some basic tools, the processing time can be radically reduced. The product
quality, processing speed and recovery parameters comparing to the traditional column based chromatography will also be discussed.
9:05 Core Bead Chromatography for Preparation of Highly Pure, Infectious Respiratory Syncytial Virus in the Negative Purification Mode
Sophia T. Mundle, Ph.D., Deputy Director, Protein Chemistry, Sanofi Pasteur
Respiratory syncytial virus (RSV) is an important human pathogen, and a frequent viral cause of respiratory disease in infants, the elderly and immunocompromised. The overall disease burden warrants the development of a safe and effective prophylactic
vaccine. One approach to vaccination against viral pathogens is the live-attenuated virus. The data which will be presented describe a scalable, chromatography-based purification procedure for preparation of highly pure, infectious live-attenuated
a Bead-Based Purification Method: Fast and Easy Isolation of Antibodies and His-Tagged Proteins
Keren Drori, Ph.D., Product Manager, Marketing, Protein Science, Takara Bio USA, Inc.
There is a constant need for faster, more efficient antibody and protein purification processes at any scale. High-capacity membrane technologies allow for purification directly from complex matrices, such as cell supernatants, in minutes. This new approach also provides highly purified and concentrated antibodies and his-tagged proteins, even from samples containing additives not compatible with other purification technologies. This talk will review several applications including purification of a GPCR, hybridoma screening, and purifying secreted protein.
10:05 Coffee Break in the Exhibit Hall with Poster Viewing
10:50 Modular Approaches for Complex Therapeutic Molecules: Reinventing Smart Bioprocessing
Stefan R. Schmidt, Ph.D., MBA, Vice President, Rentschler Biotechnology
Our concept relies on the intelligent deconvolution of general purification issues in manageable chunks that are systematically rearranged to form a logical sequence of minimally required steps to achieve the intended quality and purity profile.
Multiple modules are then assembled for each new molecule to redesign a quasi-platform downstream process. I will present the current status of our modular approach to transfer well-proven elements from platforms into downstream processes.
11:20 Case Study: Protease-Resistant Peptides for Protein Purification from Animal Plasma
Stefano Menegatti, Ph.D., Assistant Professor, Chemical and Biomolecular Engineering, North
Carolina State University
Our goal is to develop synthetic peptide ligands with high biochemical stability and selectivity for protein purification from animal sera. To this end, we have devised a combined computational/experimental framework for generating variants
of peptide ligands using non-natural amino acids. Initially, variants of antibody-binding sequences were designed and selected in silico. Our results strongly support the use of non-natural amino acids
for designing peptide ligands with enhanced biorecognition and proteolytic stability.
11:50 Bespoke Bacterial Expression Vectors and Automated 3-Dimensional Lab Scale Purification Increases Throughput and Capacity in a Drug Discovery Protein Production Facility
Christopher Gray, Ph.D., Structural Biology Team Leader, Drug Discovery Program, CRUK Beatson
The protein production section of the Beatson Drug Discovery Program supplies a considerable number of highly purified and active recombinant proteins for structural biology, biophysical and biochemistry applications. In order to minimize
any bottleneck, we have devised a series of bespoke in-house bacterial expression vectors that allow the production of proteins with multiple, protease cleavable, affinity and/or solubilizing tags resulting in parallel purification of
numerous proteins with minimal operator intervention.
12:20 pm Session Break
12:30 Luncheon Presentation:
New Technology for mAb Purification to Improve Binding Capacity and Speed
William Barrett, Ph.D., Product Specialist- Chromatography, Gore PharmBIO Products, Gore &
Protein purification can be a time-consuming process in drug discovery and research applications. Utilizing our understanding of fluoropolymer science, we’ve developed the GORE™ Protein Capture Device with Protein A. This column offers higher binding capacity at short residence time, enabling faster processing times and potential for more highly concentrated elution pools.
2:00 Chairperson’s Remarks
Stefan R. Schmidt, Ph.D., MBA, Vice President, Rentschler Biotechnology
2:05 Overload vs. Bind and Elute Cation Exchange Chromatography: A Case Study
David Glover, Senior Engineer, Purification Development, Genentech
An alternative purification approach, overload cation-exchange chromatography, has been shown to have the potential to match the impurity removal capabilities of operating in bind and elute mode while expanding the window of operation.
This talk will discuss the two operation cation-exchange chromatography modes and focus on a case study comparing and contrasting the benefits and drawbacks from both a process design and manufacturing perspective.
2:35 An Affinity Chromatography Method for Antibody Purification via Nucleotide Binding Site Targeting Ligand
Basar Bilgicer, Ph.D., Associate Professor, Chemical and Biomolecular Engineering, University
of Notre Dame
This talk describes a novel affinity chromatography technique that utilizes a small ligand that targets the nucleotide-binding site (NBS) located on Fab domain for the purification of antibodies from complex protein mixtures such as cell
culture media and ascites fluids. Results of this study established in two different solid support applications, provided high levels of antibody recovery (>98%) and purity (>98%), and yielded reproducible chromatograms maintaining
column stability over multiple injections.
3:05 Platform Purification of Viral Glycoproteins for Vaccine Development
Yingxia Wen, Ph.D., Director and Head, Protein Biochemistry, Research, Seqirus, a CSL Company
Viral surface glycoproteins play key roles for virus infection and are the main targets of immune response. Therefore they are selected as the antigens in viral vaccines. To isolate recombinant glycoproteins from mammalian cell culture and product-related contaminates, a purification platform has been developed based on the common biophysical characteristics of glycoproteins in order to accelerate vaccine development.
3:35 Refreshment Break in the Exhibit Hall with Poster Viewing
4:30 The RAS Initiative at the Frederick National Lab: Producing RAS and RAS-Binding Proteins for Structural Biology, Biochemistry, and Assay Development
William Gillette, Ph.D., Principal Scientist, RAS Protein Production, and Deputy Director,
Protein Expression Laboratory, Leidos Biomedical Research, Inc., Frederick National Laboratory for Cancer Research (FNL)
Producing proteins for experiments in XRAY crystallography, NMR, SPR, assay development, CryoEM, biochemistry, tethered by layers, and neutron scattering platforms, the RAS Initiative is working closely with a large collection of internal
and external groups to help advance knowledge on the structurally and biochemical properties of KRAS and its binding partners. My talk will review our progress and continuing challenges by presenting primary purification data and downstream
5:00 Scaling-Up of a Downstream Purification Process for a New Recombinant Product (Nuwiq)
Martin Linhult, Ph.D., Head, Bio100 Line 1, Biopharmaceuticals, Octapharma
Octapharma has developed a new process for the production of a recombinant human FVIII product derived from a human cell line (HEK293F cells). Clinical trials are ongoing with positive results. During process development, several different
approaches have been tested, old established techniques as well as new ones have been evaluated. In this presentation, I will discuss scale-up of a new downstream purification process and also different affinity ligands that could
6:20 - 7:20 Reception in the Exhibit Hall with Poster Viewing
7:20 Close of Conference