Native CZE-MS analysis of antibodies and hemoglobin using protein-adapted CZE and ESI conditions for detailed proteoform characterization
Ann-Katrin Schwenzer, Jule Weiß, Sabrina Buntz, Christian Neusüß · 2026
Read Native CZE-MS analysis of antibodies and hemoglobin using protein-adapted CZE and ESI conditions for detailed proteoform characterization by Ann-Katrin Schwenzer, Jule Weiß, Sabrina Buntz, Christian Neusüß (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/PMC13473077.txt.
Description
Ann-Katrin Schwenzer and co-authors extend a separation method for proteins in 2026, pairing electric separation with mass spectrometry. The method keeps proteins close to their natural state while sorting fine variants that differ by charge. Past work used one fixed acid level, which limited which proteins could be studied well. Here the team tunes the acid level to each protein and can switch between gentle and harsh spray fluids.
The tuned setup sorted between 45 and 100 variants for well-known antibody drugs, counting forms not reported before. Blood hemoglobin could also be split into forms that differ by sugar damage, rust-like change, or bound sulfur groups. Keeping weak bonds intact let the team see whole protein groups, not just single chains. The method offers drug makers a sharper check on product quality.
Catalog record
| CREATOR | Ann-Katrin Schwenzer, Jule Weiß, Sabrina Buntz, Christian Neusüß |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 38986 |
| LICENSE | https://creativecommons.org/licenses/by/4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |