Steady-migration retention characteristics of peptides under gradient elution： application towards a dynamic separation method for minor-adjustments of the retention of peptides in RPLC

作     者：Min Li Yongjun Lu Yicong Yang Jianjun Li Lili Wang Wei Tuo Xiaohui Ning Xin-Du Geng 

作者机构：Institute of Modern Separation Science Shaanxi Provincial Key Laboratory Northwest University Xi'an 710069 China Xi'an Aolan Science and Technology Development Company Xi 'an 710075 China Xi'an Shiyou University Xi'an 710065 China 

出 版 物：《Science China Chemistry》 (中国科学（化学英文版）)

年 卷 期：2017年第60卷第6期

页      面：829-836页

核心收录：

学科分类：081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术] 070302[理学-分析化学] 070303[理学-有机化学] 0703[理学-化学] 

基　　金：supported by the Foundation of Provincial Key Laboratory of Modern Separation Science (12JS091  13JS117  14JS096) 

主　　题：steady-migration retention liquid chromatography peptides dynamic separation minor-adjustment of retention elution orders 

摘      要：Minor-adjustment of the retention of peptides, induced by varying the mobile phase flow-rate(MPF-R), is a new dynamic separation method for simultaneously and rapidly identifying and improving the selectivity of hidden and overlapping peptide peaks. It can also-stabilize the reverse elution order of some pair-peaks under gradient elution in reverse phase liquid chromatography. The retention characteristics of peptides under gradient elution in RPLC was firstly found to be dominated by two variables of the steady region(SR) and migration region(MR). The changes in peptide retention induced by varying the MPF-R can be attributed to changes in the rate of bond breaking of multiple molecular interactions of peptides from the SR and of the mass transfer of peptides from the stationary phase to the mobile phase in the MR. The two dynamic variables were also found to independently depend on the type of peptide. Desirable results were obtained using six standard oligopeptides and a real sample of trypsin-digested *** is expected that the quality control of peptide drugs, high dispersion of peptide peaks in peptide mapping and bottom-up MSin proteomics will be improved by this method, even enabling peptide purification on a preparative scale in industry.