4.7 Article

Bioinspired dandelion-like silica nanoparticles modified with L-glutathione for highly efficient enrichment of N-glycopeptides in biological samples

Journal

ANALYTICA CHIMICA ACTA
Volume 1173, Issue -, Pages -

Publisher

ELSEVIER
DOI: 10.1016/j.aca.2021.338694

Keywords

Core-shell silica; Glycopeptides enrichment; Soft template method; Hydrophilic interaction chromatography; Thiol-ene click chemistry

Funding

  1. Key Research and Development Program of Ningxia (Special Project forForeign Cooperation) [2019BFH03004]
  2. National Natural Sciences Foundation of China [21974137]
  3. CASWeigao Research & Development Program [[2017] 0 09]

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This study successfully prepared bioinspired nano-core-shell silica microspheres as sorbents for enriching N-glycopeptides from complicated biological samples in HILIC. These microspheres exhibited great potential advantages in proteomic research by improving enrichment efficiency.
The pretreatment of complicated biological samples to eliminate the interference of nonglycopeptides and improve the efficiency of glycopeptides detection is crucial in glycoproteomics research. Hydrophilic interaction chromatography (HILIC) has been adopted for enrichment of glycosylated peptides following identification with mass spectrometry, but it is still urgent to develop novel hydrophilic materials to save cost and improve enrichment efficiency. Scientists are pursuing to fabricate freestanding intelligent artificial materials. One promising approach is to use biomimic material. In our case, one-pot strategy was developed to prepare bioinspired nano-core-shell silica microspheres (CSSMs), employing tetra-propylorthosilicate as the silicon source and phenolic resin as the soft template. The pore structure of the obtained microspheres diverged from the center to the outside with diameter ranged from 150 to 340 nm, and shell layer ranged from 25 to 83 nm by adjusting the preparation parameters. Some of them showed dandelion-like morphology. After hydrophilic modification, these CSSMs exhibited great hy-drophilicity and could be used as sorbents for enriching N-glycopeptides from complicated biological samples in HILIC. Up to 594 unique N-glycopeptides and 367 N-glycosylation sites from 182 N-glyco-proteins were unambiguously identified from 2 mL of human serum, which was superior to the enrichment performance of many HILIC materials in reported papers, demonstrating great potential advantages in proteomic application. (C) 2021 Elsevier B.V. All rights reserved.

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