Keywords

Phosphorylation Modification, Peptide, Fourier Transform Ion Cyclotron Resonance Mass Spectrometry (Ft-Icr Ms), Electron Transfer Fragmentation Mass Spectrometry (Etd Ms/Ms)

Abstract

Two peptide models (peptide A and peptide B) containing serine (S), threonine (T) and tyrosine (Y) were established, using Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR MS) and electrochemical Spray-electron transfer fragmentation mass spectrometry (LTQ-ETD MS-MS) was used to study the phosphorylated peptides obtained under dry heat conditions. FT-ICR MS analysis showed that both peptide A and peptide B introduced a phosphate group under this condition; LTQ-ETD MS-MS analysis showed that the characteristic peaks of S and Y modification of peptide A were obvious, while T was modified. The modified characteristic peaks overlap with some of the characteristic peaks where Y is modified, and it is impossible to determine whether T is phosphorylated. Phosphorylated peptide B only contains S and T. S has a very obvious modification characteristic peak, while no T is modified. Characteristic peaks. The results show that S and Y are more susceptible to phosphorylation modification than T under dry heat conditions, which may be related to the position of the hydroxyl groups on the branch chains of the three amino acids.

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Original research done by Liu Guangxian, Liu Chengmei, Tu Zongcai, Wang Hui, Xiao Hui, Chen Gang

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