2018年9月10日
Retention Order Reversal of Phosphorylated and Unphosphorylated Peptides in Reversed-Phase LC/MS
Analytical Sciences
- ,
- ,
- 巻
- 34
- 号
- 9
- 開始ページ
- 1037
- 終了ページ
- 1041
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.2116/analsci.18scp11
- 出版者・発行元
- Japan Society for Analytical Chemistry
Protein phosphorylation is one of the most ubiquitous post-translational modifications in humans, and trypsin-digested phosphorylated peptides have been analyzed by reversed phase LC/MS using C18-silica columns under acidic conditions to profile human phosphoproteomes. Here, we report that phosphopeptides generally exhibit stronger retention than their unphosphorylated counterparts when C18-silica columns are used with acetic acid or formic acid as an ion-pairing reagent, whereas the retention order is reversed when less hydrophobic stationary phases such as C4-silica columns are employed. Similarly the retention reversal is observed when more hydrophobic ion-pairing reagents such as trifluoroacetic acid are used with C18-silica columns. These phenomena could be explained by the smaller S-values of phosphopeptides in linear solvation strength theory, based on the reduced net charge caused by intramolecular interaction between phosphate and basic groups.
- リンク情報
- ID情報
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- DOI : 10.2116/analsci.18scp11
- ISSN : 0910-6340
- eISSN : 1348-2246
- Web of Science ID : WOS:000445994200009