PepTalk 2017
PepTalk 2017
2014 Archived Content

Cambridge Healthtech Institute’s Fifth Annual
Protein Aggregation and Emerging Analytical Tools
Mechanistic, Predictive, Screening and Formulation Challenges
January 16-17, 2014

This annual conference covers the latest trends, challenges and solutions in protein aggregation. It features in-depth case studies and interactive discussions on mechanisms of aggregation, detection and quantitation of aggregates, characterization tools, visible and sub-visible protein aggregation detection and analysis techniques. It will also present case studies on prevention of particle formation, impact of aggregation on production, aggregates as a factor for immunogenicity and approaches for improvement of biophysical properties of protein solutions as related to their drugability.

Day 1 | Day 2 | Download Development Brochure | Speaker Biographies 


1:00-1:45 pm Conference Registration

Mechanism of Protein Aggregation 

2:00 Chairperson’s Opening Remarks

NormGarceauNorman Garceau, Ph.D, CSO, Blue Sky BioServices, Inc.


Keynote Presentation

2:05 Mechanisms of Protein Aggregation

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

The forces that result in protein aggregation arise from various noncovalent interactions. Included in these interactions is the hydrophobic effect. This talk will focus on how the distance dependence of the hydrophobic effect may be incorporated in the proximity energy framework, and how various excipients modulate the hydrophobic effect.

2:45 The Effect of Formulation Factors on Opalescence in Protein Solutions

Ashlesha S. Raut, Ph.D. Candidate, Department of Pharmaceutical Sciences, University of Connecticut

The talk will discuss the theory of critical phenomena and the effect of formulation conditions on opalescence in protein solutions. The influence of protein-protein interactions on opalescence in the protein solutions will also be discussed.

3:15 Selected Oral Poster Presentation: Investigating Bioprocessing Variables that Influence Antibody Stability During Therapeutic IgG Production

Stephanie A. Davies, Postgraduate Research Student, Centre for Molecular Processing and School of Biosciences, University of Kent

The presence of particles and aggregates in biotherapeutic products is a concern for the manufacturers of such biologics due to the potentially associated immunogenic responses observed in some patients. In this work we have investigated the upstream and downstream bioprocess conditions that may induce or reduce IgG antibody particle formation. The two major findings from this work are firstly, varying culture stresses affects the levels of particles present in the final formulation; and secondly the inclusion of an additional wash step reduces the levels of these particles.

Wyatt3:30 The Light Scattering Toolbox for Predicting and Characterizing Aggregation

Dan SomeDaniel Some, Ph.D., Principal Scientist, Wyatt Technology Corp.

Protein aggregates arise through a variety of pathways and take on many forms. Light scattering and related instrumentation constitute a powerful suite of tools that work in tandem to characterize absolute molar mass, size, charge and interactions of simple and conjugated proteins in solution, their propensity to aggregate and final aggregation states. This talk will review how essential light scattering techniques provided by Wyatt Technology inform the R&D process for overcoming aggregation.

4:00 Refreshment Break in the Exhibit Hall with Poster Viewing


4:45 Hydrogen-Deuterium Exchange Mass Spectrometry for Measurements of Protein-Protein Interactions

Jeffrey HudgensJeffrey W. Hudgens, Ph.D., Research Chemist, Institute for Bioscience and Biotechnology Research, BioProcess Measurements Group, Biomolecular Measurement Division, NIST

Hydrogen-deuterium exchange mass spectrometry (HDX-MS) measures the exchange rates of amide hydrogens along protein chains. Since intra- and intermolecular hydrogen bonding within folded proteins can greatly slow amide hydrogen exchange, even small changes in protein tertiary structure can change the H/D exchange profile. Thus, HDX-MSprofiles report on the protein environment, including its folding configurations and binding interactions with adjacent proteins, as occurs in oligomers and aggregates.

5:15 Analytical Challenges in Detecting Protein Aggregates

Elizabeth ToppElizabeth M. Topp, Ph.D., Dane O. Kildsig Chair and Head, Department of Industrial and Physical Pharmacy, Purdue University

Aggregates are a common impurity in protein drug products, and can lead to potency changes and immunogenic response in patients. While various analytical methods can be used to detect aggregates, there is no single gold standard and different methods often give conflicting results. This presentation gives an overview of current methods for detecting and quantifying aggregates and suggests approaches for comprehensive product characterization.

5:45 Close of Day

Day 1 | Day 2 | Download Development Brochure | Speaker Biographies