Downloads: 59

Files in This Item:
File Description SizeFormat 
analsci.18SCP11.pdf128.35 kBAdobe PDFView/Open
Title: Retention Order Reversal of Phosphorylated and Unphosphorylated Peptides in Reversed-Phase LC/MS
Authors: OGATA, Kosuke  kyouindb  KAKEN_id  orcid (unconfirmed)
ISHIHAMA, Yasushi  kyouindb  KAKEN_id  orcid (unconfirmed)
Author's alias: 小形, 公亮
石濱, 泰
Keywords: Phosphopeptides
retention order reversal
linear solvation strength theory
reversed-phase LC
Issue Date: 10-Sep-2018
Publisher: Japan Society for Analytical Chemistry
Journal title: Analytical sciences : the international journal of the Japan Society for Analytical Chemistry
Volume: 34
Issue: 9
Start page: 1037
End page: 1041
Abstract: 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.
Rights: © 2018 by The Japan Society for Analytical Chemistry
DOI(Published Version): 10.2116/analsci.18SCP11
PubMed ID: 30058604
Appears in Collections:Journal Articles

Show full item record

Export to RefWorks

Export Format: 

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.