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Stepped collisional energy improves protein acylation identification by eliminating positional bias of cyclic immonium ions

文献类型：期刊论文

作者Zhu, Zhao-Yu1,4; Mao, Peng-Zhi3,4; Tarn, Ching3,4; Cao, Yong2
刊名COMMUNICATIONS CHEMISTRY
出版日期2025-12-09
卷号9期号:1页码:14
ISSN号2399-3669
DOI10.1038/s42004-025-01826-2
通讯作者Cao, Yong(ycao@siii.cas.cn)
英文摘要Mass spectrometry-based proteomics is indispensable for studying post-translational modifications. Cyclic immonium ions serve as invaluable diagnostic markers for lysine acylations, yet the principles governing their generation efficiency are poorly understood. Here, we systematically investigate this question and uncover a robust "position effect": the generation of immonium ions is strongly favored when the modified residue is located near the N-terminus of a tryptic peptide. Utilizing LysargiNase digestion and isotope-labeled synthetic peptides, we demonstrate that this effect is likely driven by the inherent instability of b-type fragment ions during collision-induced dissociation. Furthermore, we show that a stepped higher-energy collision dissociation strategy enables enhanced sequence coverage and robust cyclic immonium ion detection (similar to 99%), thereby improving the depth, reliability and speed of acylation identification. Collectively, this work provides fundamental understanding of immonium ion formation and establishes an optimized acquisition and analysis strategy that enhances the efficiency and confidence of protein acylation analysis.
WOS关键词METABOLIC-REGULATION ; CONTAINING PEPTIDES ; MASS-SPECTROMETRY ; GENE-EXPRESSION ; HCD ; ACETYLATION ; DISSOCIATION
资助项目National Natural Science Foundation of China (National Science Foundation of China)[32401236]
WOS研究方向Chemistry
语种英语
WOS记录号WOS:001662788900002
出版者NATURE PORTFOLIO
源URL[http://119.78.100.183/handle/2S10ELR8/322634]  
专题中国科学院上海药物研究所
通讯作者Cao, Yong
作者单位1.Chinese Acad Sci, Shanghai Inst Mat Med, Shanghai, Peoples R China
2.Chinese Acad Sci, Shanghai Inst Immun & Infect, Shanghai, Peoples R China
3.Chinese Acad Sci, Inst Comp Technol, Key Lab Intelligent Informat Proc, Beijing, Peoples R China
4.Univ Chinese Acad Sci, Beijing, Peoples R China
推荐引用方式
GB/T 7714		 Zhu, Zhao-Yu,Mao, Peng-Zhi,Tarn, Ching,et al. Stepped collisional energy improves protein acylation identification by eliminating positional bias of cyclic immonium ions[J]. COMMUNICATIONS CHEMISTRY,2025,9(1):14.
APA Zhu, Zhao-Yu,Mao, Peng-Zhi,Tarn, Ching,&Cao, Yong.(2025).Stepped collisional energy improves protein acylation identification by eliminating positional bias of cyclic immonium ions.COMMUNICATIONS CHEMISTRY,9(1),14.
MLA Zhu, Zhao-Yu,et al."Stepped collisional energy improves protein acylation identification by eliminating positional bias of cyclic immonium ions".COMMUNICATIONS CHEMISTRY 9.1(2025):14.

入库方式： OAI收割

来源：上海药物研究所

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