| Autor: |
Liu, Fanny C., Lee, Jusung, Pedrete, Thais, Panczyk, Erin M., Pengelley, Stuart, Bleiholder, Christian |
| Předmět: |
|
| Zdroj: |
Chemical Communications; 10/4/2024, Vol. 60 Issue 77, p10740-10743, 4p |
| Abstrakt: |
Investigating the structural heterogeneity of monoclonal antibodies is crucial to achieving optimal therapeutic outcomes. We show that tandem-trapped ion mobility spectrometry enables collision-induced unfolding measurements of subpopulations of a humanised IgGk NIST monoclonal antibody (NISTmAb). Our results indicate that differential glycosylation of NISTmAb does not modulate its conformational heterogeneity. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
|
