A metal oxide affinity probe derived from MIL-125 for selective enrichment of endogenous phosphopeptides. Issue 7 (18th February 2021)

• Record Type: Journal Article
• Authors: Zhao, Yameng; Zhang, Lingyi; Cao, Licheng; Zhang, Lei; Zhang, Weibing
• Is Part Of: Analyst. Volume 146:Issue 7(2021)
• Page Start: 2255
• Page End: 2263
• Publication Date: 2021-02-18
• Subjects: Chemistry, Analytic -- Periodicals; 543
• DOI: 10.1039/d0an02174a
• Languages: English
• ISSNs: 0003-2654

Abstract

Abstract : Highly effective enrichment of endogenous phosphopeptides from complex biological samples is an essential and crucial theme in the analysis of phosphopeptidomics. Abstract : Highly effective enrichment of endogenous phosphopeptides from complex biological samples is an essential and crucial theme in the analysis of phosphopeptidomics. Herein, an ordered mesoporous TiO2 /C composite (denoted as Ti–MCM) was prepared by the pyrolysis of MIL-125 under a N2 atmosphere. The obtained Ti–MCM possesses a high specific surface area (165 m 2 g −1 ), a uniform pore size (3.75 nm), and a large amount of Ti (46%). By utilizing the selective chelation between Ti–MCM and phosphopeptides, 25 phosphopeptides were detected in α-casein digest after enrichment. The material shows good selectivity even in the presence of 2000-fold excess of interference peptides. It was also used to enrich endogenous phosphopeptides from the complex samples of human serum and saliva and showed a good performance.