2017 Archived Content

THURSDAY, 16 NOVEMBER | 17:30 - 20:30 | DINNER

Protein Aggregation: Mechanism, Characterization and Consequences

Instructor:

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

Introduction

Protein aggregation is recognized by regulatory agencies and the biopharmaceutical industry as a key quality attribute of biotherapeutic products. Various aggregates hold the potential for adversely impacting production and patients in a variety of ways. This in-depth workshop reviews the origins and consequences of aggregation in biotherapeutics, and then examines strategies for predicting and quantifying aggregation in biopharmaceuticals. It benefits scientists engaged in development, production, analytical characterization and approval of biotherapeutics and who require a good working knowledge of protein aggregation.

Topics Include:

  • What are the causes of protein aggregation
  • How much influence does the solvent have on aggregation
  • What protein features are responsible
  • What changes may be made to the protein to improve solubility
  • What changes to the solvent may be made
  • How do the changes impact solubility
  • How does the proximity energy framework provide insights into the causes of aggregate formation, and how can it help guide you to a better formulation

Instructor Bio:

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

Dr Thomas Laue is the Carpenter Professor of Molecular, Cellular and Biomedical Sciences, and professor of Material Sciences at the University of New Hampshire. He is the Director of the Center to Advance Molecular Interaction Science, and is the founder and Director emeritus of the Biomolecular Interaction Technologies Center. His research focuses on the development of instrumentation and methods that use the fundamental properties of mass and charge for characterizing macromolecular interactions