ac8b00461_si_005.xlsx (40.4 kB)
Two-Dimensional MoS2‑Based Zwitterionic Hydrophilic Interaction Liquid Chromatography Material for the Specific Enrichment of Glycopeptides
dataset
posted on 2018-05-09, 00:00 authored by Chaoshuang Xia, Fenglong Jiao, Fangyuan Gao, Heping Wang, Yayao Lv, Yehua Shen, Yangjun Zhang, Xiaohong QianMass spectrometry
(MS)-based glycoproteomics research requires
highly efficient sample preparation to eliminate interference from
non-glycopeptides and to improve the efficiency of glycopeptide detection.
In this work, a novel MoS2/Au-NP (gold nanoparticle)–L-cysteine
nanocomposite was prepared for glycopeptide enrichment. The two-dimensional
(2D) structured MoS2 nanosheets served as a matrix that
could provide a large surface area for immobilizing hydrophilic groups
(such as L-cysteine) with low steric hindrance between the materials
and the glycopeptides. As a result, the novel nanomaterial possessed
an excellent ability to capture glycopeptides. Compared to commercial
zwitterionic hydrophilic interaction liquid chromatography (ZIC-HILIC)
materials, the novel nanomaterials exhibited excellent enrichment
performance with ultrahigh selectivity and sensitivity (approximately
10 fmol), high binding capacity (120 mg g–1), high
enrichment recovery (more than 93%), satisfying batch-to-batch reproducibility,
and good universality for glycopeptide enrichment. In addition, its
outstanding specificity and efficiency for glycopeptide enrichment
was confirmed by the detection of glycopeptides from an human serum
immunoglobulin G (IgG) tryptic digest in quantities as low as a 1:1250
molar ratio of IgG tryptic digest to bovine serum albumin tryptic
digest. The novel nanocomposites were further used for the analysis
of complex samples, and 1920 glycopeptide backbones from 775 glycoproteins
were identified in three replicate analyses of 50 μg of proteins
extracted from HeLa cell exosomes. The resulting highly informative
mass spectra indicated that this multifunctional nanomaterial-based
enrichment method could be used as a promising tool for the in-depth
and comprehensive characterization of glycoproteomes in MS-based glycoproteomics.