Publications by authors named "Markus Bluemel"

Protein aggregation, which takes place both in vivo and in vitro, is an important degradative pathway for all proteins. Protein aggregates have distinct physicochemical and biological properties that are important to study and characterize from the perspective of both fundamental and applied sciences. The size of protein aggregates varies across a huge range, spanning several orders of magnitude.

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Purpose: Accurate monitoring of the sub-visible particle load in protein biopharmaceuticals is increasingly important to drug development. Manufacturers are expected to characterize and control sub-visible protein particles in their products due to their potential immunogenicity. Light obscuration, the most commonly used analytical tool to count microscopic particles, does not allow discrimination between potentially harmful protein aggregates and harmless pharmaceutical components, e.

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Since each antibody has its unique physical chemical properties, optimal formulation for one antibody is likely not applicable for the others. To rapidly screen multiple antibody formulations, an automated system was constructed to perform sample preparation, testing, and data management. Using the automatic system, up to 500 liquid formulations can be prepared in deep well microplates and further distributed into standard microplates that can be stored under different stress conditions for degradation studies.

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