Protein stability measurements amplified: Combining SEC-MALS and DLS to maximize data output
The stability of a protein sample and its tendency to aggregate is explored using a combination of SEC-MALS and DLS
Protein stability measurements amplified: Combining SEC-MALS and DLS to maximize data output
The stability of a protein sample and its tendency to aggregate is explored using a combination of SEC-MALS and DLS
Introduction
All biopharmaceuticals are subject to extremely high regulatory burdens that must be met to show their efficacy and safety. One particular area of regulatory scrutiny for biologics is their stability and the level of aggregate material that they contain. Tools that can be used to study protein stability and aggregation provide valuable information for regulators and assist developers to produce safe, reliable, high quality products. Using orthogonal technologies for complementary analyses increases confidence in the resulting data.
Size exclusion chromatography (SEC) and light scattering are two workhorse techniques for biopharmaceutical stability and aggregation analysis. SEC is regularly used to assess the aggregation state of protein samples throughout the drug development pipeline. Static light scattering (often referred to as multi-angle light scattering (MALS) is used to measure protein molecular weight (MW). Dynamic light scattering (DLS) is used to detect early aggregates and also to monitor aggregate formation in response to stimuli such as time or raised incubation temperatures. These two techniques used together provide a wealth of important information about the stability and aggregation profile of a sample, whilst conserving sample volume and operator time and effort.
