Methionine oxidation (revision 2)
Old revision·10:26, 11 Nov 2024·ColumnOvenCoy
This is an old revision of this page, as it stood at 10:26, 11 Nov 2024, saved by ColumnOvenCoy with the summary rm the claim that the method is stability-indicating without a forced-degradation study. It may differ substantially from the current revision, and any error it contains may since have been corrected.
| Methionine oxidation | |
|---|---|
| Residue affected | Methionine; cysteine and tryptophan by related routes |
| Mass change | +16 Da (sulfoxide); +32 Da (sulfone) |
| Promoted by | Peroxides, trace metals, light, dissolved oxygen |
| Topic infobox · conventions | |
Methionine oxidation converts the thioether side chain of methionine to a sulfoxide, adding 16 daltons, and on further oxidation to a sulfone, adding 32. It is one of the most common oxidative degradation routes in peptides and is readily detected by mass spectrometry because the mass shift is large.[1]
Oxidation is promoted by dissolved oxygen, by trace transition metals, by peroxide impurities in excipients, and by light. Unlike deamidation, which proceeds spontaneously in clean aqueous solution, oxidation generally requires an oxidant, and controlling the oxidant is therefore an effective control strategy.[2]
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