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

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Conference Short Courses*View Details 

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

  • Characterization and Analysis of Particulates
  • Protein Crystallization - Delineating Protein Structure
  • DoE and QbD: Tools for Optimizing the Bioprocess

Tuesday, January 11 - 4:30 pm - 7:30 pm

  • Dynamic Light Scattering - Theory, Do's & Don'ts, and  Data Interpretation

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

  • Rational Design of Protein Solutions

 

THURSDAY, JANUARY 13


1:00 pm Conference Registration

 

Mechanisms of Protein Instability

1:45 Chairperson’s Opening Remarks

Ramil Latypov, Ph.D., Senior Scientist, Process and Product Development, Amgen, Inc.

1:50 Coping with the Colloidal Properties of Proteins

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

Often it is useful to consider the colloidal properties of a protein when considering how best to formulate it. This talk will describe the colloidal properties of proteins and how the solvent can be used to optimize solubility and viscosity. Experimental approaches will be described that are useful for determining the colloidal properties. The audience will gain a systematic understanding of the colloidal properties of proteins; ways to measure those properties; and guides for how solvent properties can influence the colloidal properties.

2:20 Novel Oxidative and Photolytic Pathways of Protein Degradation

Christian Schoneich, Ph.D., Professor, Chair, Department of Pharmaceutical Chemistry, University of Kansas

Protein aggregation and fragmentation represent important degradation pathways with potential long-term consequences such as immunogenicity. Here, we will present a series of novel degradation pathways of pharmaceutically relevant proteins such as immunoglobulins and growth hormone originating from Cys oxidation and/or disulfide reduction and photolysis, which ultimately form chemically stable ether and thioether cross-links. A mechanistic analysis of these pathways was performed with specifically designed model peptides.

2:50 Aggregation and Self-Association in a High Concentration Antibody Solutions

Devendra (Davy) S. Kalonia, Ph.D., Professor of Pharmaceutics, University of Connecticut

This talk will focus on the importance of solution properties of a monoclonal antibody at high concentrations. The effect of pH and ionic strength on self association and aggregation depends on the nature of the protein-protein interactions in solution. Application and limitations of multiple techniques to measure protein-protein interactions will also be discussed.

3:20 Sponsored Presentation (Opportunity Available)

3:35 Refreshment Break, Exhibit and Poster Viewing

 

Measuring and Improving Stability

4:30 Measuring and Increasing Protein Stability

C. Nick Pace, Ph.D., Professor, Medical Biochemistry &Genetics; Biochemistry and Biophysics, Texas A&M

Increasing conformational stability of proteins has been an important goal. I will discuss the methods that can be used to measure the conformational stability of proteins. In vitro selection has been used to increase protein stability, but most often site-directed mutagenesis is used to optimize the various forces that contribute to protein stability. I will discuss the most successful approaches based on site directed mutagenesis that can be used to stabilize proteins. In addition, I will discuss non-mutagenic approaches that can be used to stabilize proteins.

5:00 Towards Understanding Ion-Induced Protein Aggregation: Correlation with Biophysical Predictors of Stability

Yatin Gokarn, Ph.D., Associate Director, Late-Stage Pharmaceutical and Process Development, Genentech

The presentation will attempt to elucidate the underlying mechanism(s) governing ion-induced interactions in antibodies and related basic proteins. Case studies focused on studying the effect of ions on agitation and temperature induced aggregation and reversible self-assocation will be presented. The use of biophysical tools for predicting aggregation propensity and viscoelastic properties of mAbs will also be discussed.

5:30 Engineering, Characterizing and Formulating Aggregation-Resistant Antibodies

Peter M. Tessier, Ph.D., Assistant Professor, Department of Chemical & Biological Engineering, Center for Biotechnology & Interdisciplinary Studies, Rensselaer Polytechnic Institute

The significance of aggregation continues to grow with increasing demands for high concentration antibody formulations. We are pursuing three key approaches to address this problem: 1) Improve selection of antibodies; 2) reengineer existing antibodies; and 3) identify superior formulation conditions. Each of these ambitious pursuits is currently limited by the lack of understanding of how antibody sequence and structure influence aggregation, as well as a lack of high-throughput methods for identifying antibody variants or formulation conditions that minimize aggregation. In this presentation, we will discuss our work towards addressing each of these challenges.

6:00 Close of Day


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Links to Companion Meetings

Pipeline 1

Optimizing Biologics Formulation Development 

Protein-Device Combinations 

Lyophilization, Spray Drying & Emerging Drying Technologies


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

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      Premier Sponsors: 

EMD Millipore 

 Novozymes (white) 

PerkinElmer NEW 2009 

 Protein Simple  

  

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Training Seminars 

Mon-Tues, January 13-14 

Biologics Formulation and Delivery  

 


Buzz Sessions
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