Abstract
Isotopic labeling of peptides by trimethylation creates a charged quaternary amine group on the peptide that provides clear differentiation from unlabeled protonated peptides and protonated or sodiated chemical background. Differential mobility spectrometry, with its use of a chemical modifier, allows otherwise undesirable ion/molecule reactions in the mobility cell to increase selectivity and sensitivity of quantitative peptide analysis. A high proton affinity modifier selectively removes protonated and sodiated interference and background ions by proton and sodium transfer, while leaving the trimethylated ions with their quaternary amine groups unchanged.
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