January 18-22, 2016 | Town and Country Resort Hotel | SAN DIEGO, CA 
January 18-22, 2016 | Town and Country Resort Hotel | SAN DIEGO, CA 

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Cambridge Healthtech Institute’s 8th Annual
Protein Purification and Recovery
Streamlining Processes with Innovative Technologies
January 19-20, 2016

Protein purification is the most costly and time-consuming process in the manufacturing of proteins. Challenges are multiplied when purifying complex molecules, such as membrane proteins, bispecifics and antibody-drug conjugates. The Protein Purification and Recovery conference explores 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 also address alternatives and breakthroughs, such as continuous processing. This leading purification meeting includes a highlighted session focused on purifying membrane proteins, and addresses optimizing processes to ensure purity and quality.

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Final Agenda


1:00 pm Conference Registration


2:00 Chairperson’s Opening Remarks

William Gillette, Ph.D., Senior Scientist, Protein Expression Laboratory, Cancer Research Technology Program, Leidos Biomedical Research, Inc., Frederick National Laboratory for Cancer Research (FNL)


2:05 Making Water-Soluble Integral Membrane Proteins in vivo Using an Amphipathic Protein Fusion Strategy

Matthew_DeLisaMatthew P. DeLisa, Ph.D., William L. Lewis Professor, Chemical & Biomolecular Engineering, Cornell University

Here we devise a general strategy for in vivo solubilization of IMPs in structurally relevant conformations without the need for detergents or mutations to the IMP itself. This technique, called SIMPLEx (solubilization of IMPs with high levels of expression), allows the direct expression of soluble products in living cells by simply fusing an IMP target with truncated apolipoprotein A-I, which serves as an amphipathic proteic ‘shield’ that sequesters the IMP from water and promotes its solubilization.

⊲ Featured Presentation
2:45 Expression and Sample Preparation of Membrane Proteins for Structure Determination by NMR

Stanley_OpellaStanley Opella, Ph.D., Professor, Chemistry and Biochemistry, University of California, San Diego

The advantages of heterologous expression of proteins in bacteria include the ability to make relatively large amounts and the ready incorporation of stable isotopes. The use of a hydrophobic fusion protein enables the sequestration in inclusion bodies to avoid damaging the cell membrane.

3:15 Refreshment Break in the Exhibit Hall with Poster Awards

4:00 Overcoming the Purification Challenges with Bone Morphogenetic Proteins

Robertson_PatrickPatrick Robertson, Ph.D., Senior Scientist, Purification Development, FUJIFILM Diosynth Biotechnologies

The distinctive nature of bone morphogenetic proteins creates unique challenges in purification, such as low solubility near physiological pH and a tendency to aggregate and/or precipitate in the presence of salts limiting the design space for developing an effective and scalable purification strategy. We will present an approach that leverages their unique structural characteristics in purification development.

4:15 Sponsored Presentation (Opportunity Available)

4:30 It Takes Two to Tango—Structure/Function Studies Yield the Dance of the Permease

Ronald_KabackH. Ronald Kaback, M.D., Distinguished Professor, Physiology, University of California, Los Angeles

Lactose permease (LacY) catalyzes translocation of a galactoside and an H+ across the membrane. X-ray structures, and structure/function studies reveal that: (1) LacY utilizes an alternating access mechanism; (2) sugar binding involves induced fit; (3) Active transport does not involve a change in KD for sugar on either side of the membrane, but the pKa decreases markedly. (4) Transport is driven chemiosmotically, and ∆µ̃H+ acts kinetically to accelerate the process.

5:00 Strategies for High Yield Affinity Purification of Functional G Protein Coupled Receptor from Detergent Solutions

Alexei_YeliseevAlexei Yeliseev, Ph.D., Staff Scientist, LMBB, NIH/NIAAA

Human cannabinoid receptor CB2, a G protein-coupled receptor involved in regulation of immune response, is an important target for pharmaceutical drug development. We expressed the functional CB2 receptor in E. coli, and optimized its purification by tandem affinity chromatography using novel affinity resins StrepTactin XT Superflow and EF2 Ca-calbindin-based resin. Examples of successful purification and efficient recovery (over 80%) of CB2 from dilute detergent-containing solutions will be presented.

5:30-5:45 Short Course Registration

5:45-8:45 Dinner Short Courses

Recommended Short Course: SC11: Protein Aggregation: Mechanism, Characterization and Consequences – Detailed Agenda  

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8:00 am Conference Registration and Morning Coffee


8:30 Chairperson’s Remarks

Patrick Robertson, Ph.D., Senior Scientist, Purification Development, FUJIFILM Diosynth Biotechnologies

8:35 Purification of Common-Light-Chain Bispecific Antibodies

Juergen_NettJuergen Nett, Ph.D., Associate Director, High Throughput Expression, Adimab, LLC

A variety of bispecific constructs benefit from the use of a single variable light region pairing with multiple distinct variable heavy regions. This talk will demonstrate new techniques to purify these common-light-chain bispecific IgG molecules to homogeneity. A panel of bispecific constructs are then generated that bind to each target with high affinity and exhibit favorable biophysical properties similar to traditional therapeutic antibodies.

9:05 A Simple, Robust Two-Column Purification Platform for Antibody Fragment Manufacturing

Green_ZhangGreen Guihang Zhang, Ph.D., Director, Protein Sciences, ImaginAb, Inc.

Minibody and cys-diabody are unique types of antibody fragments developed for clinical imaging. Purification of minibodies and cys-diabodies has proved to be challenging due to their high aggregation and low-pH sensitivity. We have recently developed a simple and robust two-column purification platform for manufacturing minibody and cys-diabody for clinical applications with high purity and stability. The same platform may be used for other types of antibody fragment purification.

9:35 Sponsored Presentation (Opportunity Available)

10:05 Coffee Break in the Exhibit Hall with Poster Viewing

10:50 Developing a Purification Platform for FAB

Jiansheng Wu, Ph.D., Senior Scientist, Protein Chemistry, Genentech, Inc.

FAB has gained more attention in recent years due to its broad applications in therapeutics and diagnostics. Generating grams level of FAB from E.coli cell pellets is important for many preclinical studies. We evaluated several resins for FAB purification and developed a robust purification platform to obtain up to 20 grams of FAB from E. coli cells.

11:20 The Challenges of Developing a Purification Process for Bispecific Protein Product for Early Phase Clinical Trial

Yun Bai, Ph.D., Director, Process Development, Ambrx, Inc.

11:50 Aggregation Challenges during the Purification Development of a Low pl Monoclonal Antibody
Sandra Rios, Ph.D., Principal Scientist, Process Development & Engineering, Merck

Monoclonal antibodies typically have a high degree of homology and similar physicochemical properties leading to utilization of platform processes for production and purification. However, there are instances where significant modifications to these processes are needed due to uncommon characteristics, such as low pI and aggregation propensity. In this study, process buffers, intermediate stability, and optimization of multiple polishing chromatography steps were required to mediate the protein behavior to develop a suitable purification process. 


12:20 pm Sponsored Presentation (Opportunity Available)

12:50 Session Break

1:00 Luncheon Presentation (Sponsorship Opportunity Available) or Enjoy Lunch on Your Own


2:00 Chairperson’s Remarks

Jiansheng Wu, Ph.D., Senior Scientist, Protein Chemistry, Genentech, Inc.

2:05 Purification of Secretory IgA from Lemna minor (Duckweed)

Danielle_van_WijkDaniëlle van Wijk, Ph.D., Lead Scientist / Project Leader, Down Stream Processing, Synthon Biopharmaceuticals B.V.

Here we present the duckweed Lemna minor as a promising platform for production of SIgA antibodies. The production process comprises (1) expression of SIgA in stably-transformed duckweed; (2) extraction of SIgA by disruption of the plant material; (3) removal of naturally abundant impurities by acidic precipitation; (4) clarification by depth filtration and TFF; (5) purification by affinity chromatography followed by polishing steps; and (6) formulation in a stable buffer.

2:35 Protein Purification for the RAS Initiative at the Frederick National Lab

Bill_GilletteWilliam Gillette, Ph.D., Senior Scientist, Protein Expression Laboratory, Cancer Research Technology Program, Leidos Biomedical Research, Inc., Frederick National Laboratory for Cancer Research (FNL)

One of the major goals of the RAS Initiative at the Frederick National Lab is to deepen the knowledge of the RAS proteins. In support of that effort, the Protein Expression Laboratory has focused its effort on the purification of KRAS4b, its oncogenic mutants, and interacting protein partners in a multidisciplinary effort. Biophysical characterization and functional assays of the proteins will be discussed.

3:05 The Use of Affinity Tags to Overcome Obstacles in Recombinant Protein Expression and Purification

Jian-Ping_JinJian-Ping Jin, M.D., Ph.D., Professor and William D. Traitel Endowed Chair, Physiology, Wayne State University School of Medicine

To overcome obstacles in the expression and purification of recombinant proteins are of importance in research and industrial applications. A strategy is the use of affinity tags or carrier peptide. Strategies have also been developed to remove the tag after purification and obtain native protein and peptide products. There are unsolved problems and imperfect applications. The pros and cons of current approaches will be discussed for improvement and future development.

3:35 Refreshment Break in the Exhibit Hall with Poster Viewing


4:30 Crystallization as a Tool for Scalable, Efficient Purification Techniques in Early Process Step for Purifying Recombinant Proteins

Partha_HazraPartha Hazra, Ph.D., Chief Scientific Manager, Research, Biocon

Crystallization/precipitation can be a simplified, efficient and cost effective tool for separation of both process and product related impurities in processing of recombinant therapeutic proteins. I will present a Case Study comparing traditional Capture chromatography and Crystallization/precipitation steps, and will cover the advantages of one over the other when manufacturing at large scale. Comparative quality observed in the scale up experiences also will be covered in the case study.

5:00 pH-Dependent Sharkbodies for Affinity Purification of Biologics

Harald_KolmarHarald Kolmar, Ph.D., Professor and Head, Applied Biochemistry, Chemistry, Technical University of Darmstadt

We have established a platform for generation of shark-based antibody domains that display pH-dependent target protein binding. To this end, a master library of sharkbodies with random histidine-enriched binding loops was generated that are displayed on yeast cells and screened by high-throughput FACS. Due to their high inherent stability and pH-dependent binding characteristics they are excellently suited for affinity chromatography purification of biologics, particularly for non-antibody protein therapeutics.

5:45 BuzZ Session B

Join your peers and colleagues for interactive roundtable discussions.

6:30-7:30 Reception in the Exhibit Hall with Poster Viewing

7:30 Close of Conference

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