Abstract
To investigate the side-chain effects of O-phosphorylation on the peptidyl-prolyl amide bond cis/trans isomerization, a series of model phosphopeptides with Xaa-Pro motif were designed and synthesized. Electrospray Ionization Mass Spectrometry (ESI-MS) and Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry (MALDI-TOF-MS) experiments were performed to study the differences between these two methods in their fragmentation behaviors on the phosphopeptides. It was found that the loss of fragment at m/z 98 was observed not only in the ESI-MS spectra but also in the MALDI spectra, which was due to the loss of phosphate derivatives. The loss of small molecules such as ammonia and water was easier in ESI-MS spectrum. Moreover, the peptidyl-prolyl amide bonds (Xaa-Pro) in the phosphopeptides were prone to cleave in both ESI-MS and MALDI-TOF-MS spectra. The results presented here indicated that ESI-MS was more suitable for small molecule analysis while MALDI-MS was more effective in detection of peptides backbone.
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