Water Proton NMR: A Tool for Protein Aggregation Characterization
| Autor: | Y. Bruce Yu, Marc B. Taraban, Brian Lobo, Roberto A DePaz |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
Magnetic Resonance Spectroscopy
02 engineering and technology Protein aggregation 030226 pharmacology & pharmacy Analytical Chemistry Protein Aggregates 03 medical and health sciences 0302 clinical medicine Dynamic light scattering Freezing Water proton Particle Size Chromatography Chemistry Temperature Antibodies Monoclonal Water Nuclear magnetic resonance spectroscopy 021001 nanoscience & nanotechnology Dynamic Light Scattering Characterization (materials science) Dilution Cuvette Chromatography Gel Particle size Protons 0210 nano-technology |
| Zdroj: | Analytical Chemistry. 89:5494-5502 |
| ISSN: | 1520-6882 0003-2700 |
| Popis: | Formulation stability is a critical attribute of any protein-based biopharmaceutical drug due to a protein’s inherent tendency to aggregate. Advanced analytical techniques currently used for characterization of protein aggregates are prone to a number of limitations and usually require additional manipulations with the sample, such as dilution, separation, labeling, and use of special cuvettes. In the present work, we compared conventional techniques for the analysis of protein aggregates with a novel approach that employs the water proton transverse relaxation rate R2(1H2O). We explored differences in the sensitivity of conventional techniques, size-exclusion chromatography (SEC), microflow imaging (MFI), and dynamic light scattering (DLS), and water NMR (wNMR) toward the presence of monoclonal antibody aggregates generated by different stresses. We demonstrate that wNMR outperformed SEC, DLS, and MFI in that it was most consistently sensitive to increases in both soluble and insoluble aggregates, includ... |
| Databáze: | OpenAIRE |
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