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Buzz Session 

PepTalk's BuzZ Sessions are focused discussions in which delegates discuss important and interesting biotherapeutic related topics from upstream protein expression and production through downstream scale-up and manufacturing. This is a moderated discussion with brainstorming and interactive problem solving between scientists from diverse areas who share a common interest in the discussion topic.

BuzZ Session A | BuzZ Session B


BuzZ Session B: 

Tuesday, January 22nd, 2013
3:30 – 4:15 pm


TABLE 22B: Next Generation Half-Life Extension:  Is "Tunability" Desired and if so, How Would One Go About It?

Randall Engler, Director, Strategic Accounts, Novozymes, Inc.

  • What HLE technologies offer a tunability feature?
  • Some organizations are pursuing monthly dosing for some drugs; are there downsides to this effort?
  • Are there regulatory challenges in such an approach that are different from other?

TABLE 23B: Selective Protein Quantification with Spectrophotometry

Philippe Stas, CEO, Trinean NV

  • UV-VIS protein quantification for purified proteins only?
  • Industry needs for novel quantification methods
  • Alternatives for spectrophotometry

TABLE 24B: Affinity Tags in Expression and Purification of Membrane Proteins

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

  • Use of tandem affinity tag purification
  • Tags for purification of membrane receptors
  • Novel methods of purification

TABLE 25B: The Potential Role of Self-Cleaving Tag Technologies in Biopharmaceutical Manufacturing

David W. Wood, Ph.D., Associate Professor, Chemical and Biomolecular Engineering, Ohio State University

  • Available technologies, advantages and disadvantages of each
  • Process design and process considerations
  • Potential regulatory issues and process validation

TABLE 26B: Finding a Suitable Expression System for the Production of Your Protein

Heidi Roschitzki-Voser, Ph.D., Senior Scientist, Biochemistry Institute, University of Zurich

  • Prokaryotic expression systems: E. coli, L. lactis...
  • Eukaryotic expression systems: -Insect cell (Sf9, Tn5) – mammalian cells (COS, HEK293, HEK293T, HEK293S Gnt-, ...)

TABLE 27B: Extending the Half-Life of Peptide Therapeutics

Volker Schellenberger, Ph.D., CEO and President, Amunix

  • Overview of half-life extension technologies
  • What are strengths and limitations of each approach?
  • Chemical conjugation versus recombinant fusion
  • Half-life extension versus slow release
  • Regulatory hurdles

TABLE 28B: Linkers in Recombinant Fusion Proteins

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

  • Expression and production
  • Biological activity and efficacy
  • Pharmacokinetics
  • Other properties of fusion proteins

TABLE 29B: Using Recombineering for DNA Fabrication

JrGang Cheng, Ph.D., Associate Professor, Center for Neuroscience, University of North Carolina Chapel Hill

  • Which system to use: recombinogenic bacteria or plasmids?
  • Concerns with the modification of high copies plasmids
  • Working with large construct such as BAC (Bacteria Artificial Chromosome) for transgenesis
  • Challenge of bacteria chromosome editing beyond E. coli

TABLE 30B: High-Level Secreted Expression of Therapeutic Proteins / Enzymes in Pichiapastoris (or yeasts in general)

Roland Weis, Ph.D., Head of Operations, VTU Technology

  • Are yeasts still "weirdos" for protein production?
  • N-glycosylation and other PTMs
  • High throughput methods for microbial eukaryotic protein production
  • Novel accomplishments with Pichia/yeasts

TABLE 31B: Engineering Protein Therapeutics for Device Compatibility

Bob Kelley, Ph.D., Senior Scientist, Drug Delivery, Genentech

  • Early sequence evaluation for high concentration formulation and stability
  • Overcoming instability in physiological conditions
  • Need for improved computational and experimental methods forstudying proteins at high concentration
  • Animal models for uptake from subcutaneous space
  • Understanding clearance from ocular tissue

TABLE 32B: QbD in Freeze Drying and Design of the Freezing Process

Michael Pikal, Ph.D., Pfizer Distinguished Endowed Chair in Pharmaceutical Technology & Professor of Pharmaceutics, University of Connecticut

  • What is "Design Space"?
  • What is the role of "Design of Experiments" in QbD for Freeze DriedProteins?
  • What is the meaning of "Validation" within the contest of QbD?

TABLE 33B: Pulmonary Delivery of Drugs/Vaccine

Tarun Mandal, Ph.D., McCaffrey/Norwood Endowed Professor of Pharmacy & Director, Center for Nanomedicine & Drug Delivery, College of Pharmacy, Xavier University of Louisiana

  • Is the pulmonary delivery right for your molecule?
  • Delivery via oral vs. nose
  • Local vs. systemic action
  • Impact of particle size on lung deposition

TABLE 34B: Detection of Protein Aggregation in the Solid State

Evgenyi Shalaev, Ph.D., Research Investigator, Allergan

  • Protein aggregation is a major stability issue in various systems, such as during storage of freeze-dried formulations or in controlled release dosage forms (e.g., PLGA microspheres)
  • Protein aggregation is usually measured after a solid material is dissolved
  • It would be important to detect if protein aggregates are formed in the solid state

TABLE 35B: Strategies for Dose Reduction

David Meininger, Ph.D., Executive Director, Molecular Discovery, Merck

  • Enabling active transport into target tissue
  • CMC engineering
  • Catabolic/pH-sensitivity engineering

TABLE 36B: Multipass Membrane Protein Monoclonal Antibody Discovery

James W. Stave, Ph.D., Senior Research Fellow, SDIX

  • Membrane-dependent epitopes, topology and size of extracellular loops
  • Orthologs and immunogenicity
  • Immunization and screening strategies
  • Single cell isolation, mab gene cloning and expression strategies
  • Epitope mapping, mab diversity and function

TABLE 37B: Utilizing Microenvironments to Improve CHO Results

Kevin Sunley, Ph.D., Senior Scientist, XBiotech USA

  • Understanding microenvironment components
  • Choosing the most pliable environments
  • Applying the results to expression

TABLE 38B: How to Use Modeling to Improve CHO Production Outcomes

Kyongbum Lee, Ph.D., Associate Professor & Acting Chair, Department of Chemical & Biological Engineering, Tufts University

  • Choosing the correct model
  • Data analysis for enhanced outcomes
  • What the model should tell you

TABLE 39B: External Sourcing Strategic Objectives

Brian Cain, Ph.D., Key Account Executive, Sales, Blue Sky Biotech, Inc.

  • Can strategic outsourcing be used to help increase innovation?
  • What best practices exist to utilize strategic outsourcing to increase innovation and can they also be used to help increase output?
  • How can outsourcing fit into your current strategy?

TABLE 40B: How Can Label-Free Binding Analysis Technologies Such as BLI and SPR be More Useful in Characterizing Protein and Antibody Therapeutics?

Sriram Kumaraswamy, Ph. D., Global Director of Applications, Marketing, Pall FortéBio

  • Areas where label-free assays are currently used in your organization for biotherapeutics discovery and characterization
  • Benefits accrued from adopting label-free assays
  • Assays that are currently on your wish list for addressing through label-free technology

TABLE 41B: Decreasing Costs through Industry/University Cooperative Centers

Thomas Laue, Ph.D., Professor, Biochemistry and Molecular Biology; Director, Biomolecular Interaction Technologies Center (BITC), University of New Hampshire

  • What are I/UCRCs and how do they function?
  • What are their immediate and long-term benefits to companies?
  • What sort of research fits well

TABLE 42B: Incorporating Human Factors

Moderator: R. Reade Harpham, Manager, Human Centric Design, Battelle Memorial Institute

  • Understand the difference between Human Factors research and Market Research
  • Why Human Factors is here to stay
  • Lessons Learned – What NOT to do

BuzZ Session A | BuzZ Session B