PepTalk 2017
PepTalk 2017

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Cambridge Healthtech Institute’s second annual “Protein Aggregation: Understanding and Overcoming Analytic, Formulation, Manufacturing, and Regulatory Challenges” covers the latest trends and challenges with a focus on: understanding and controlling protein aggregation, improving detection and quantitation of aggregates, analyzing subvisible and visible particles with various techniques, utilizing complimentary technologies for characterization, developing approaches for rational design/protein engineering of aggregation-resistance for proteins, understanding aggregates as an inducing factor in immungenicity, improving structural analysis and modeling to predict protein aggregation, and understanding the impact of primary sequence and refolding potential on aggregation. The conference features novel case studies, in-depth scientific presentations, and poster sessions. Time has been designated for interactive discussions with industry thought leaders during the BuzZ Sessions on Tuesday and panels. It is part 2 of 3 within the “Pipeline 1: Formulating Biologics: Meeting the Challenges” track and is perfect for those new to the field, as well as those who require in-depth analysis of the latest trends, technologies, and techniques.

Recommended Pre-Conference Short Course*

Sunday, January 10

(SC1) Immunogenicity Assessment: Preclinical, Clinical and Post-Marketing

* Separate registration required 

Tuesday, January 12


Arrive early and join BuzZ Session Roundtable Discussions, Poster Awards and Short Courses!

2:00 Buzz A

2:45 Networking Refreshment Break in the Exhibit Hall

3:15 Poster Awards in the Exhibit Hall

3:30 Buzz B

4:15 Close of Optimizing Biologics Formulation Development

4:15 Registration for Short Courses

4:30 – 7:30 Concurrent Short Courses (SC 5 – SC 8)

Recommended Short Course
(SC5) Characterization and Analysis of Particulates

* Separate registration required 


Wednesday, January 13

7:00 am Registration for Protein Aggregation

7:30 Breakfast Presentation (Sponsorship Opportunity Available) or Morning Coffee



8:15 Chairperson’s Opening Remarks

Hung-Wei Chih, Ph.D., Early Stage Pharmaceutical Development, Genentech


Understanding and Controlling Protein Aggregation: Experimental Approach and Lessons Learned from Various Protein Formulation Case Studies

Wolfgang Fraunhofer, Ph.D., Group Leader, Associate Research Fellow, Global Pharmaceutical and Analytical Development, Abbott Bioresearch Center

Coping with aggregation is a challenging task during the development and life-cycle management process of protein pharmaceuticals. A practical approach for the selection of both suitable stress experiment set-up and appropriate analytical techniques for characterizing and understanding general physical stability and protein aggregation is presented. Data of various preclinical, clinical, and commercial stage protein formulation case studies will be presented and discussed.

9:00 Protein Aggregation: A Case Study of Process Understanding

Carol F. Kirchhoff, Ph.D., Senior Principal Scientist, Pharmaceutical R&D, Global Biologics, Pfizer, Inc.

9:30 Determination of Reversible Self-Association at High Protein Concentration and its Impact on Viscosity

Steven J. Shire, Ph.D., Staff Scientist and Group Leader, Process R&D, Genentech, Inc.

Reversible protein self-association has been linked to high viscosity of a monoclonal antibody (MAb) high concentration formulation (Liu et al. , J. Pharm. Sci. 2005). We have used rheological measurements, preparative analytical sedimentation equilibrium and static light scattering to investigate the impact of salts and ionic strength on the self association and viscosity of closely related IgG1 MAbs at concentrations >100 mg/mL. These experiments suggest that ionic attractive interactions result in an orientation of IgG1 molecules, which at high concentration result in high viscosity values. Theses closely related MAbs were constructed from the same human IgG1 Fc constructs, and thus the major differences exist between the different complementarity regions (CDRs) of these MAbs. In order to further explore the impact of different amino acid residues in the CDRs, and their impact on self-association and viscosity a series of charge swap mutants were created, and the initial results will be discussed.

10:00 Networking Coffee Break in the Exhibit Hall


Aggregation at Surfaces and During Cold/Cryo Storage

10:45 Stabilization of Protein against Surface Adsorption-Induced Aggregation

Li Shi, Ph.D., Senior Director, Technology Development, Genzyme, Inc.

The goal of formulation research is to develop safe, efficacious, stable, and scalable dosage forms. The challenges for achieving this goal for an aqueous protein formulation include the intrinsic lability of proteins and the stabilization of bulk drug substances and drug products in solution or in parenteral dosage form against various storage, handling, and process stresses. This session discusses stable protein bulk solution characterization and formulation development as well as the mechanism of the stabilization. Topics include: characterization of protein intrinsic properties; stabilization of proteins in solution through stabilizing excipient screening; mechanism of protein stabilization in solution by non-ionic surfactants.

11:15 Understanding Cryoconcentration Effects during Freeze/Thaw Processing of Bulk Protein and Possible Consequences on Protein Aggregation

Parag Kolhe, Ph.D., Principal Scientist, Global Research and Development, Global Biologics, Pfizer, Inc.

Freezing and thawing of bulk protein solutions is important due to the flexibility afforded in terms of maximizing productivity and enabling drug product logistics. Freezing eliminates risk from shaking/agitation stresses during transport and minimizes the possibility of microbial growth. However, freezing-induced protein aggregation due to cryoconcentration, eutectic crystallization of buffer solutes, and resulting pH changes, ice-water surface denaturation offer significant challenges for success with this unit operation. In this proposal, a case study will be presented that encompasses the fundamental understanding of freezing and thawing in current available technologies from cryoconcentration as well as solute distribution perspective and its effect on possible aggregation.

11:45 Characterizing Aggregates Formed During Cold Storage

Jamie Moore, Ph.D., Scientist and Group Leader, Early Stage Pharmaceutical Development, Genentech, Inc.

Frozen storage can be an effective method for long-term stabilization of therapeutic proteins. This presentation will discuss the impact of freezing rates and storage temperature conditions on protein stability during long-term frozen storage.

12:15 pm Close of Morning Session

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



2:00 Chairperson’s Remarks

Pete Tessier, Ph.D., Assistant Professor, Chemical & Biological Engineering, Rennsaelaer Polytechnic Institute

2:05 Enabling Analytical Methods for Extractables and Leachables Testing for Biologics

Nanda Subbarao, Ph.D., Senior Consultant, Analytical-CMC, Biologics Consulting Group

Extractables/Leachables include non-volatiles, semi-volatiles, volatiles, and trace metals. Non-volatiles E/L chemicals can be tested by HPLC-MS whereas volatiles would need to be tested by GC-MS. Trace metal residues require Atomic Spectroscopy. Methods of the appropriate sensitivity and specificity must be chosen in order to reach meaningful conclusions for the E/L study. The sensitivity and specificity of some commonly used methods and some promising emerging tools will be presented.

2:35 Subvisible and Visible Particle Analysis by Light Obscuration and Flow Imaging Techniques

Quanmin Chen, Ph.D., Scientist, Process Biochemistry & Formulation Sciences, MedImmune, Inc.

3:05 Field-Flow Fractionation as a Possible Tool for Analyzing Protein Aggregates

Tsumoto Kouhei, Ph.D., Associate Professor, Division of Frontier Biosciences, University of Tokyo

Several analytical tools have been proposed as a possible method for analyzing protein aggregates. Field-Flow Fractionation is one of the best candidates. Here, I will talk about how we can use FFF for the analyses, and also application of this method to analyzing several proteins will be reported.

3:35 Sponsored Presentation (Sponsorship Opportunity Available)

3:50 Networking Refreshment Break


Mechanisms of Protein Instability, Aggregation, and Immunogenicty

4:30 Antibody-Drug-Conjugate: Why is the Drug Falling off?

Hung-Wei Chih, Ph.D., Early Stage Pharmaceutical Development, Genentech

5:00 Predicting Protein Aggregation Prone Regions: Implications for the Design of Therapeutic Proteins with Enhanced Stability

Naresh Chennamsetty, Ph.D., Post-Doctoral Associate, Chemical Engineering, Massachusetts Institute of Technology

Co-developed with Bernhardt Trout, Ph.D., Director, Novartis-MIT Center for Continuous Manufacturing,Professor, Department of Chemical Engineering, Massachusetts Institute of Technology

A new tool called ‘spatial-aggregation-propensity (SAP)’ is presented for predicting protein aggregation prone regions. The tool is based on molecular simulations, which is validated by designing antibodies through genetic engineering that are significantly more stable than the wild type. The tool described here has the potential to enable the therapeutic use of antibodies that are currently too unstable. Furthermore, it could be used to incorporate developability in a rational way during the screening of antibodies in the discovery phase.

5:30 Reception in the Exhibit Hall

6:30 Close of Day


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