Reproducibility of Thermally Induced and Contact-stir Induced Protein Aggregation

This peer-reviewed publication by Fluence Analytics’ research partner Tulane PolyRMC addresses the reproducibility of protein aggregation. The publication, which appears in the Journal of Physical Chemistry, specifically discusses reproducibility following temperature-induced and contact-stir induced aggregation of bovine serum albumin and a monoclonal antibody. Using ARGEN, PolyRMC assessed protein aggregation reproducibility for global stressors which affect an entire protein population, such as temperature, and for local stressors that only affect a partial population, such as stirring. Because all 16 ARGEN cells are completely independent, researchers were able to use varying degrees of thermal stress, contact stirring, and non-contact stirring simultaneously. The publication also discusses whether aggregation is inherently deterministic, stochastic, or chaotic.

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