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Peptide science

Oxidation of methionine and cysteine

Methionine oxidises readily, gaining a single oxygen atom. It is one of the most common degradation routes in peptide storage.

What happens

The sulfur in a methionine side chain reacts with oxygen to form methionine sulfoxide, adding 16 daltons to the molecular mass. That mass shift is detectable by mass spectrometry, which is how oxidation is usually identified.

Cysteine oxidises too, forming disulfide bonds either within a chain or between chains. Inter-chain bonds produce dimers and higher aggregates.

What drives it

Dissolved oxygen, trace metal ions that catalyse the reaction, light, and elevated pH all accelerate oxidation. Peroxide impurities in solvents are another route, which is one reason solvent quality matters.

What limits it

Keeping material dry and cold, protected from light, and limiting exposure to air. Each vial entry admits fresh oxygen, so repeated entry accelerates the process in a way continuous cold storage does not.

Consequence

An oxidised peptide is a different molecule. Whether that matters depends entirely on the experiment, but it is a real change to what is in the vial and not merely a cosmetic one.

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