Use of Water Proton NMR to Characterize Protein Aggregates: Gauging the Response and Sensitivity
| Autor: | Marc B. Taraban, Roberto A DePaz, Y. Bruce Yu, Brian Lobo |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Transverse Relaxation Rate
Range (particle radiation) Aggregate (composite) Chemistry 010401 analytical chemistry Size-exclusion chromatography Analytical chemistry Protein aggregation 010402 general chemistry 01 natural sciences 0104 chemical sciences Analytical Chemistry Dynamic light scattering Water proton Sensitivity (control systems) |
| Zdroj: | Analytical Chemistry. 91:4107-4115 |
| ISSN: | 1520-6882 0003-2700 |
| Popis: | Water proton transverse relaxation rate R2(1H2O) measurements by NMR stand out as a powerful noninvasive tool to detect protein aggregates, including subvisible particles in biopharmaceutical formulations. To understand the applicability of water proton NMR (wNMR), we studied the response and sensitivity of wNMR to the aggregates of a monoclonal antibody (mAb) within a wide size range at different aggregate levels, for three different physical stresses: freeze–thaw cycling, heating, and agitation. We compared the sensitivity and response of wNMR with those observed by conventional techniques of size exclusion chromatography (SEC), microflow imaging (MFI), and dynamic light scattering (DLS). Our findings showed that wNMR detects mAb aggregates within wide aggregate levels and in a wide range of aggregate sizes. wNMR was sensitive to an increase in soluble protein aggregates in the range of |
| Databáze: | OpenAIRE |
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