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Development of high‐throughput and high sensitivity capillary gel electrophoresis platform method for Western, Eastern, and Venezuelan equine encephalitis (WEVEE) virus like particles (VLPs) purity determination and characterization
Author(s) -
Gollapudi Deepika,
Wycuff Diane L,
Schwartz Richard M,
Cooper Jonathan W,
Cheng KC
Publication year - 2017
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.201700217
Subject(s) - capillary electrophoresis , repeatability , chromatography , relative standard deviation , chemistry , monoclonal antibody , detection limit , antibody , biology , immunology
In this paper, we describe development of a high‐throughput, highly sensitive method based on Lab Chip CGE‐SDS platform for purity determination and characterization of virus‐like particle (VLP) vaccines. A capillary gel electrophoresis approach requiring about 41 s per sample for analysis and demonstrating sensitivity to protein initial concentrations as low as 20 μg/mL, this method has been used previously to evaluate monoclonal antibodies, but this application for lot release assay of VLPs using this platform is unique. The method was qualified and shown to be accurate for the quantitation of VLP purity. Assay repeatability was confirmed to be less than 2% relative standard deviation of the mean (% RSD) with interday precision less than 2% RSD. The assay can evaluate purified VLPs in a concentration range of 20–249 μg/mL for VEE and 20–250 μg/mL for EEE and WEE VLPs.