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Abstract
Free radical-initiated peptide sequencing (FRIPS), a TEMPO-assisted mass spectrometry, has shown potential as a peptide tandem mass spectrometry (MS/MS) tool that can be an alternative to electron-based mass spectrometry and the traditional collision-based methods. However, a couple of instrumentation barriers need to be overcome before this approach can be a practical tool. One of the barriers is the limitation of the FRIPS-based technique to ion trap mass spectrometry or an orbitrap due to the MS3 workflow. To overcome this challenge, the work introduces a recently developed activation within the trapped ion mobility mass spectrometry (TIMS) device that was found to initiate the radical species. More importantly, the generated product ion was mobility separated, which increased the sequence coverage. Overall, coupling the activation within the TIMS cell with the para-TEMPO-Bz-based FRIPS mass spectrometry offers another practical approach that can be utilized for peptide MS/MS analysis.
Supplementary materials
Title
Supporting information.
Description
Supplementary material includes TIMS activation process, additional CIDtims mass spectra of substance P, angiotensin I, and angiotensin II at 30 and 130 V, CIDtims mass spectra, mobility spectra, and 2D-IMS-MS plot of β-amyloid (10-20), substance P, and angiotensin II, additional CIDtims fragment ions and mobility resolved product ions of para-conjugated ACTH (1-14), mobility resolved mass spectrum of ACTH (1-14), β-amyloid (10-20), and substance P, FRIPS MS/MS mass spectra of conjugated peptides following CID and HCD, and mass error (ppm) tables.
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