Characterizing Protein Aggregates and Higher Order Structures using AUC - Technical Seminar Sponsored by Beckman Coulter Life Sciences

In the half century since the first crystallography derived structure of a protein; structural biology has blossomed into a mature discipline exploring the correlation between structure, dynamics and function of proteins. The latest frontier in structural biology is the study of higher order structures (HOS) of proteins and their complexes. This is of particular relevance in biopharma where the quantification of different HOS species is directly correlated to determining the dosage and efficacy of the therapeutic protein.

Analytical ultracentrifugation (AUC) is one of the most versatile biophysical tools used today for the characterization of biological samples ranging from small drug molecules to intact viruses, vesicles and microparticles. AUC works with biological samples in the native state and does not depend on a matrix, reporter species or custom-coated substrates. AUC separates biomolecules based upon both size, molecular mass and anisotropy and can also be used to quantify interactions between different species. In this talk, we will discuss the principles of AUC and discuss the workflow to characterize the presence of HOS/aggregate species in an antibody sample. We will also touch upon other centrifugation instruments used in a typical protein purification and characterization workflow.