Protein aggregation is currently one of the leading problems in formulation of therapeutic proteins. Aggregates reduce efficacy and cause immunogenicity.  Pharmaceutical companies are interested in new techniques that enable high throughput screens for optimizing formulations that minimize protein heterogeneity. Current methods such as native polyacrylamide gel electrophoresis (PAGE), size-exclusion chromatography (SEC) and capillary electrophoresis (CE) are time consuming and limited in how many samples can be run in parallel.  Our approach involves the use of fast sieving electrophoresis of proteins in sub-micron non-porous silica bearing brush layers of polyacrylamide. These can be miniaturized to give separations of therapeutic monoclonal antibodies in a few mm, potentially enabling a 96 well plate format.

Towards a high throughput method for rapidly sizing protein drugs in formulations

246th National Meeting (2013)

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