Are you interested in techniques suitable for studying aggregates and supramolecular assemblies? If so, take a look at this presentation.

Protein aggregation in biotherapeutic drugs is a major concern as they affect the effective dosage and may cause immunogenic responses in patients. However, a lack of reliable analytical methods has hindered the quantification of submicron (0.1 to 1 mm) protein aggregates and a detailed understanding of their formation kinetics.

Separation Science, in collaboration with Wyatt Technology, brings you an on-demand presentation that describes a simple asymmetrical flow field-flow fractionation (AF4) method used to investigate nanometer and submicron aggregates of heat-stressed anti-streptavidin (anti-SA) IgG1. This talk, given by Dr Kim Williams (Colorado School of Mines), show cases the importance of a separation technique when studying complex and dynamic systems. Questions about the impact of a separation method on potentially 'labile' analytes is also addressed.

To view this presentation, and other related talks, click on the link below:
http://bit.ly/2UOZ9Yd

Kim Williams is a Professor of Chemistry at the Colorado School of Mines. Her research area can be broadly classified as separation science of nanometer to beyond micrometer-size analytes. This includes a focus on developing field-flow fractionation (FFF) with light scattering approaches to simultaneously separate and characterize complex multi-component systems. Her current projects address questions pertaining to protein aggregation kinetics and stability, lipidomics of lipoproteins, and thermal diffusion of polymers and colloids and how this transport process can yield important analytical information pertaining to composition and architecture/morphology.