文献类型：期刊文献

英文题名：Retention mechanism and enrichment of glycopeptides on titanium dioxide

作者：Sheng, Qianying[1];Li, Xiuling[2];Yin, Wei[3];Yu, Long[2];Ke, Yanxiong[1];Liang, Xinmiao[1,2]

机构：[1]E China Univ Sci & Technol, Engn Res Ctr Pharmaceut Proc Chem, Minist Educ, Sch Pharm, Shanghai 200237, Peoples R China;[2]Chinese Acad Sci, Dalian Inst Chem Phys, Key Lab Separat Sci Analyt Chem, Dalian 116023, Peoples R China;[3]Dalian Maritime Univ, Dalian 116026, Peoples R China

年份：2013

卷号：5

期号：24

起止页码：7072

外文期刊名：ANALYTICAL METHODS

收录：;EI(收录号：20134917046700);WOS:【SCI-EXPANDED(收录号:WOS:000327506600028)】；

基金：This work was supported by the National High Technology Research and Development Program of China (863 Program, 2012AA020203), State Key Program of National Natural Science of China (21135005) and National Science Foundation of China (21105100, 21205116 and 30801513).

语种：英文

外文关键词：Hydrophilicity - Molecular biology - Peptides

摘要：A uniform method for the facile and selective enrichment of glycopeptides with titanium dioxide (TiO2) is presented. Retention mechanisms between glycopeptides and TiO2 were explored by checking the influence of acetonitrile content, NH3 center dot H2O concentration and formic acid concentration on the retention of glycopeptides. Both hydrophilic interaction and ligand-exchange retention mechanisms between glycopeptides and TiO2 were found to be involved. Based on this, a uniform method was established for selective enrichment of glycopeptides with TiO2. The developed method exhibited high selectivity for N-linked glycopeptides with short to long peptide sequences. This efficient and uniform method will be a valuable tool for post-translational modification in proteomics.