Protein aggregation typically results from conformational or colloidal instability. Conformational stability is the difference in free energy (ΔG) between folded and unfolded states. While not direct assessments of free energy, melting temperature value (Tm) and aggregation temperature (TAgg) can be utilized as qualitative measurements of conformational stability.
Colloidal stability is calculated by balancing repulsive and attractive intermolecular interactions among protein molecules to sustain the native folded state. Less intermolecular interaction reduces the aggregation propensity. Thus, quantifying the second virial coefficient (B22) is an important screening tool for predicting aggregation propensity.
ARGEN™ is the perfect instrument for assessing quantitative and qualitative characteristics of all classes of biotherapeutics and determining TAgg, B22, molecular weight (Mw), alongside differences in weight, average molecular weight (aggregation) in a variety of thermal, chemical, and mechanical stressors. The following article summarizes the way ARGEN™ is used to calculate the second virial coefficient (B22) and molecular weight (Mw) of a monoclonal antibody.
ARGEN is an extremely efficient instrument for rapidly assessing the stability and viability of therapeutic proteins, peptides, and biopolymers. The tool features a multi-stressor testing platform that detects static light scattering and processes intuitive data. These characteristics allow researchers to make biologic formulations up to 16 times more quickly.
ARGEN uses fixed angle (90°), SMSLS (simultaneous multiple sample light scattering) technology, which delivers fast, instantaneous, continuous data collection for defining qualitative and quantitative characteristics of target molecules. The instrument has 16 independently controlled sample cells, allowing users to simultaneously set up thermal, chemical, and mechanical stirring stress parameters on all samples. This makes way for an extremely versatile approach to experimental design.
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