Facile preparation of polymer-grafted ZIF-8-modified magnetic nanospheres for effective identification and capture of phosphorylated and glycosylated peptides. Issue 38 (10th September 2020)

• Record Type: Journal Article
• Authors: Yi, Linhua; Yan, Yinghua; Tang, Keqi; Ding, Chuan-Fan
• Is Part Of: Analytical methods. Volume 12:Issue 38(2020)
• Page Start: 4657
• Page End: 4664
• Publication Date: 2020-09-10
• Subjects: Chemistry, Analytic -- Periodicals; Analytical biochemistry -- Periodicals; Chemical laboratories -- Standards -- Periodicals; 543.1905
• DOI: 10.1039/d0ay01412e
• Languages: English
• ISSNs: 1759-9660

Abstract

Abstract : As a member of MOFs, Zn-MOFs (ZIF-8) are seldom used in phosphopeptide enrichment because ZIF-8 is soluble in acid solutions. Abstract : As a member of MOFs, Zn-MOFs (ZIF-8) are seldom used in phosphopeptide enrichment because ZIF-8 is soluble in acid solutions. Therefore, properly designing a novel strategy to overcome the defect of ZIF-8 is necessary. In this study, a novel multifunctional nanoprobe was designed by uniting magnetic core, titania shell and hydrophilic metal–organic frameworks (named as Fe3 O4 @PDA@mTiO2 @PEI- g -ZIF-8). Integrating the strategies of hydrophilic interaction affinity chromatography (HILIC), immobilized metal ion affinity chromatography (IMAC) and metal oxide affinity chromatography (MOAC), the Fe3 O4 @PDA@mTiO2 @PEI- g -ZIF-8 mesoporous microspheres can enrich phosphorylated peptides and glycosylated peptides simultaneously. Fe3 O4 @PDA@mTiO2 @PEI- g -ZIF-8 has high selectivity (maximum molar ratio β-casein/HRP : BSA = 1 : 1000), low detection limit (2 fmol) towards phosphopeptides and glycopeptides. Besides, the Fe3 O4 @PDA@mTiO2 @PEI- g -ZIF-8 also exhibited a fine performance in the actual sample detection. In the experiment, taking saliva as a sample, 16 phosphorylated peptides were identified, and from a human serum sample, 4 phosphorylated peptides were selectively identified. All in all, the materials show great potential in the future study of phosphoproteomics and glycoproteomics.