High-efficiency recognition and identification of disulfide bonded peptides in rat neuropeptidome using targeted electron transfer dissociation tandem mass spectrometry
Yu, XiDivision of Biological Technology, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, China
Khani, AbbasVisual Cognition Laboratory, Department of Medicine, University of Fribourg, Switzerland
Ye, XuetingShenyang Pharmaceutical University, Shenyang, China
Petruzziello, FilomenaVisual Cognition Laboratory, Department of Medicine, University of Fribourg, Switzerland
Gao, HuiyuanShenyang Pharmaceutical University, Shenyang, China
Zhang, XiaozheDivision of Biological Technology, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, China
Rainer, GregorVisual Cognition Laboratory, Department of Medicine, University of Fribourg, Switzerland
Analytical Chemistry. - 2015, vol. 87, no. 23, p. 11646–11651
English
The main goal of the present study is to develop a method to recognize and identify endogenous intrachain disulfide bonded peptide, which are rarely sequenced in current peptidomics studies. In order to achieve highly efficient detection of these peptides in a neuropeptidome analysis, we alkylated the peptides, mined the raw mass spectrometry data, and then recognized the candidates of untreated disulfide bonded peptides from unalkylated peptide extracts. After removing more than 90% features, targeted electron transfer dissociation fragmentation was performed for detecting and fragmenting disulfide bonded peptides, and even most of them were present in low abundance in the original sample. Diverse endogenous disulfide bonded peptides were then detected and sequenced, opening up new perspectives for comprehensively understanding the response of a neuropeptidome.