PepTalk 2017
PepTalk 2017


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