Identifying Tryptophan Oxidation in Antibodies
Author Information
Author(s): Hensel Miriam, Steurer Rebecca, Fichtl Juergen, Elger Carsten, Wedekind Frank, Petzold Andreas, Schlothauer Tilman, Molhoj Michael, Reusch Dietmar, Bulau Patrick
Primary Institution: Roche Diagnostics GmbH, Penzberg, Germany
Hypothesis
Can we identify specific sites of tryptophan oxidation in recombinant antibodies using tert-butylhydroperoxide and quantitative LC-MS?
Conclusion
The study successfully identified a specific tryptophan residue in a recombinant IgG1 antibody that is susceptible to oxidation under certain conditions.
Supporting Evidence
- The study identified a solvent accessible tryptophan residue in the CDR of a recombinant IgG1 antibody.
- Oxidation levels of tryptophan were found to be significant compared to other residues.
- The developed method allows for efficient identification of oxidation sites in antibodies.
Takeaway
The researchers found a part of an antibody that can get damaged over time, which can affect how well the antibody works. They used a special method to see where this damage happens.
Methodology
The study used tert-butylhydroperoxide to induce oxidation in a recombinant IgG1 antibody, followed by quantitative LC-MS for analysis.
Limitations
The study primarily focused on a single tryptophan residue and may not represent all oxidation sites in antibodies.
Digital Object Identifier (DOI)
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