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•Application Note: Protein Aggregation Monitoring On The FLUOstar OPTIMA Microplate Reader

The importance of studying protein aggregation becomes apparent when we realize that not only is it the underlying cause of many debilitating and often incurable human diseases1 but that it is also one of the most significant obstacles to the development of protein-based therapeutics; aggregation during drug formulation invariably leads to reduced efficacy, low yield, poor storage capacity, and increased production costs.

The ability to understand why and how proteins aggregate will undoubtedly help improve upon current strategies aimed at eliminating the causes and effects of this phenomenon. This may sound easy but the reality is that, due to the unique structural and physicochemical properties (e.g. thermodynamic stability, hydrophobicity, and net protein charge) of the vast numbers of proteins described to-date, the conditions required to induce protein aggregation are often highly protein-specific and are as varied as the proteins themselves.

Compounding this problem is the existence of the many biophysical factors (e.g. temperature, pH, molecular crowding, sequence mutations, proteolysis, and molecular chaperones) that also have profound influences on protein aggregation. With such an array of aggregation determinants at hand, the task of assessing what effect one or more of these factors have on the aggregation of a given protein would be almost impossible if not for the availability of firmly established screening techniques such as those that make use of multi-well microplate readers.

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•Application Note: Protein Aggregation Monitoring On The FLUOstar OPTIMA Microplate Reader

SOURCE: BMG LABTECH, GmbH