文献类型：期刊文献

英文题名：Utilizing 4-Sulfonylcalix[4]arene as a Selective Mobile Phase Additive for the Capture of Methylated Peptides

作者：Shi, Jie[1];Xiong, Yuting[2];Li, Junyan[1];Gao, Baolei[1];Qing, Guangyan[2];Sheng, Qianying[1];Lan, Minbo[1]

机构：[1]East China Univ Sci & Technol, Sch Chem & Mol Engn, Shanghai Key Lab Funct Mat Chem, Shanghai 200237, Peoples R China;[2]Chinese Acad Sci, Dalian Inst Chem Phys, Natl Chromatog R&A Ctr, State Key Lab Med Prote,CAS Key Lab Separat Sci An, Dalian 116023, Peoples R China

年份：2025

卷号：97

期号：4

起止页码：2428

外文期刊名：ANALYTICAL CHEMISTRY

收录：;EI(收录号：20250517781819);WOS:【SCI-EXPANDED(收录号:WOS:001406887000001)】；

基金：This project was supported by the Science and Technology Commission of Shanghai Municipality (STCSM, 21JM0010400), the National Key R&D Program of China (grant no. 2022YFC3400800), the National Natural Science Foundation of China (22174138), and the DICP Innovation Funding (DICP-I202243 and I202229).

语种：英文

外文关键词：Mammals - Methylation

摘要：Protein methylation has attracted increasing attention due to its significant regulatory roles in various biological processes. However, the diversity of methylation forms, subtle differences between methylated and nonmodified sites, and their ultralow abundances pose substantial challenges for capturing and isolating methylated peptides from biological samples. Herein, we develop a chromatographic method that utilizes 4-sulfonylcalix[4]arene (SC4A) as a mobile phase additive and Click-Maltose as the stationary phase to separate methylated/nonmethylated peptides through the adsorption of the SC4A-K(Me3) complex. By utilization of the interaction between calix[4]arene cavities and trimethylated lysine residues, methylated peptides could be specifically separated from peptide samples. This method significantly improves the signal-to-noise ratio (S/N), even in samples containing a 10-fold excess of bovine serum albumin (BSA) trypsin digests. Additionally, we successfully enriched 12 methylated peptides from histone digests. This study paves the way for the selective enrichment of lysine methylated peptides in post-translational modification proteomics (PTMs), enhancing both the capture efficiency and selectivity of methylated peptides and providing robust technical support for subsequent proteomics research.