文献类型：期刊文献

英文题名：Hydrophilic Phytic Acid-Coated Magnetic Graphene for Titanium(IV) Immobilization as a Novel Hydrophilic Interaction Liquid Chromatography-Immobilized Metal Affinity Chromatography Platform for Glyco- and Phosphopeptide Enrichment with Controllable Selectivity

作者：Hong, Yayun[1];Zhao, Hongli[1];Pu, Chenlu[1];Zhan, Qiliang[1];Sheng, Qianying[1];Lan, Minbo[1,2]

机构：[1]East China Univ Sci & Technol, Sch Chem & Mol Engn, Shanghai Key Lab Funct Mat Chem, Shanghai 200237, Peoples R China;[2]East China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China

年份：2018

卷号：90

期号：18

起止页码：11008

外文期刊名：ANALYTICAL CHEMISTRY

收录：;EI(收录号：20183705793409);WOS:【SCI-EXPANDED(收录号:WOS:000445322800051)】；

基金：This research was financially supported by the Science and Technology Commission of Shanghai Municipality (STCSM, No. 16520710800) and the Fundamental Research Funds for the Central Universities (No. 222201817022).

语种：英文

外文关键词：Titanium compounds - Affinity chromatography - Molar ratio - Casein - Lanthanum compounds - Ion chromatography - Nanocomposites - Peptides - Graphene - Metals

摘要：In this work, multifunctional Ti4+-immobilized phytic acid-modified magnetic graphene (denoted as MagG@PEI@PA-Ti4+) nanocomposites were fabricated through a facile route for simultaneous/respective enrichment of N-glyco- and phosphopeptides. Phytic acid (PA), with six phosphate groups, possesses excellent hydrophilicity and metal ion coordination ability, which endowed the MagG@PEI@PA-Ti4+ with combined properties of immobilized metal ion affinity chromatography (IMAC)- and hydrophilic interaction liquid chromatography (HILIC)-based materials. On the basis of the different binding ability of N-glyco- and phosphopeptides on MagG@PEI@PA-Ti4+, the MagG@PEI@PA-Ti4+ nanocomposites could enrich N-glyco- and phosphopeptides simultaneously or respectively by using different enrichment conditions, achieving controllable selective enrichment of N-glyco- and phosphopeptides. The proposed nanocomposites demonstrated an outstanding performance for selective enrichment of N-glycopeptides (selectivity, 1:1000 molar ratios of IgG/BSA; sensitivity, 0.5 fmol/mu L IgG; loading capacity, 300 mg g(-1); recovery, >90%) and phosphopeptides (selectivity, 1:5000 molar ratios of alpha-casein/BSA; sensitivity, 0.1 fmol/mu L alpha-casein; loading capacity, 100 mg g(-1); recovery, >90%). Taking advantage of these merits, a total of 393 N-glycopeptides derived from 259 glycoproteins and 574 phosphopeptides derived from 341 phosphoproteins were identified from 200 mu g of HeLa cell extracts through a single-step enrichment using MagG@PEI@PA-Ti4+.