• Mass Spectrometry Letters
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• v.4 no.4
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• pp.71-74
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• 2013

In the present study, we report that the charge-directed (assisted) peptide dissociation products, such as b- and y-type peptide backbone fragments, were the major products in MS/MS and $MS^3$ applications of some o-TEMPO-Bz-C(O)-peptide ions, while radical-driven dissociation products, such as a/x and c/z-type fragments, were previously shown to be the major products in the free radical initiated peptide sequencing mass spectrometry (FRIPS MS). Those o-TEMPO-Bz-C(O)-peptides share a common feature in their sequences, that is, the peptides do not include an arginine residue that has the highest proton affinity among free amino acids. The appearance of b- and y-type fragments as major products in FRIPS MS can be understood in terms of the so-called "mobile-proton model". When the proton is highly mobilized by the absence of arginine, the chare-directed peptide dissociation pathways appear to be more competitive than the radical-driven dissociation pathways, in our FRIPS experiments.

• Mass Spectrometry Letters
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• v.9 no.2
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• pp.56-60
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• 2018

In this study, matrix-assisted laser desorption/ionization (MALDI) was applied to the TEMPO-assisted FRIPS for the first time. We found that 3-HPA is the optimal matrix for the analysis of p-TEMPO-Bz-Sc-peptides, which gives minimal precursor fragmentations. MALDI-TOF/TOF experiments on p-TEMPO-Bz-Sc-peptides yielded mainly $[a_n+H]^+$, $[z_n+H]^+$, and $[y_n]^+-type$ products, indicating that radical-driven peptide fragmentation occurs in MALDI-TOF/TOF-MS.