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Cambridge Healthtech Institute’s 6th Annual
Protein Aggregation and Emerging Analytical Tools
Mechanism, Prediction, Screening, Immunogenicity and Formulation Challenges
January 22-23, 2015


The popular Protein Aggregation and Emerging Analytical Tools conference covers 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 and detection and analysis techniques. It also presents case studies on prevention of particle formation by engineering and formulation approaches, impact of aggregation on production, aggregates as a factor for immunogenicity and approaches for improvement of biophysical properties of protein solutions.

We invite you to join colleagues from around the world in this discussion of the key challenges and solutions in protein aggregation, and see how experts like you are overcoming analytic, formulation, manufacturing and regulatory challenges to create a stable formulation.


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Final Agenda 


THURSDAY, JANUARY 22

11:30 am Conference Registration

12:30 pm Luncheon Presentation (Sponsorship Opportunity Available) or Enjoy Lunch on Your Own

1:30 Ice Cream Break in the Exhibit Hall with Poster Viewing


Understanding Protein Interactions for Better Product Design and Development

2:00 Chairperson’s Opening Remarks


Keynote Presentations

2:05 Protein-Solvent Interaction and Its Importance to Solubility and Viscosity

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

Proteins interact with the surrounding solvent in both specific and non-specific ways. The hydration shell must be displaced for protein-protein interactions to occur. Also, proteins bind monovalent ions, particularly anions, which will affect protein-protein interactions. Previous work provides insights into how these protein-solvent interactions may impact protein solubility and viscosity. These insights are useful for guiding protein design and solvent selection.

2:45 Aggregation of Antibody CH2 Domains and Antibody-Drug Conjugates

Dimiter S. Dimitrov, Ph.D., Senior Investigator, Protein Interaction Group, FNLCR, NCI, National Institute of Health

Aggregation of isolated antibody domains will be overviewed and our recent work on CH2 and updates will be discussed (Gong R at al Mol Pharm. 2013, unpublished). Aggregation of antibody-drug conjugates (ADCs) will be discussed. Experimental data and computational models will be presented for some ADCs including those generated in our group.


3:15 Stable Human IgG Therapeutics through Engineering of Antibody Variable Domains

Daniel Christ, Ph.D., Head Antibody Therapeutics, Immunology, Garvan Institute of Medical Research

Human antibody variable domains (VH and VL) that mediate the interaction with antigen often display poor stability and a propensity to aggregate. We have recently developed generally applicable phage display and X-ray crystallography strategies that allow the stability engineering of human variable domains. Here we outline the application of the technology to full-length human IgG, and present examples of how the approach can be utilised for the ‘retrofitting’ of candidate molecules and biobetters.

3:45 Sponsored Presentation (Opportunity Available)

4:15 Refreshment Break in the Exhibit Hall with Poster Viewing


Characterization of Protein Aggregates

5:00 Detection and Characterization of Visible, Subvisible Particles and Other Aggregates: Achievements and Challenges

Anacelia Rios Quiroz, MSc, Assistant Scientist, Late-Stage Pharmaceutical and Process Development, Pharmaceutical Development & Supplies, PTD Biologics Europe, F. Hoffmann-La Roche Ltd.

The talk will give an overview of required and commercially available counting methodologies for detection of protein aggregates and visible and sub visible particles (SbVP); species ubiquitously present in protein formulations. Focus will be SbVP as they are gaining attention regarding immunogenicity and quality attributes. Lack of a well-defined methodology for SbVP makes important to increase our knowledge of emerging instruments’ performance. Applicability towards the assessment of a meaningful array of particle counting techniques will be discussed.

5:30 Characterization of Protein Aggregate Structure with SAXS

Anette Henriksen, Ph.D., Principal Scientist, Protein Biophysics and Formulation, Novo Nordisk

Proteins can aggregate through a number of different mechanisms, possibly leading to different structure and biological activity of the aggregates. We have investigated the structure of a mAb dimer by Small Angle X-ray Scattering coupled to Size Exclusion Chromatography. The results clearly show that the internal structure of the monomer is conserved to a high degree, and furthermore provide information on the relative orientation of the monomers within the dimer.

6:00-7:00 Reception at the Tiki Pavilion



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