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A carbon nanoparticles-based solid-phase purification method facilitating sensitive MALDI-MS analysis of permethylated N-glycans.

ABSTRACT: In recent decades, MALDI-MS has been extensively used for the analysis of glycans. However, native glycans usually have low ionization efficiency in MS, which hinders the direct analysis. Permethylation of glycans is a solution for this issue, but a significant amount of salt is introduced during this process, which can further suppress the MS signals. Thus, it is necessary to purify the glycans prior to MALDI-MS analysis. In this study, we developed a carbon nanoparticles-based solid-phase purification method to enable direct MALDI-MS analysis of permethylated glycans. Two carbon nanomaterials, carbon nanoparticles (CNPs) and graphene nanosheets (GNs), and two conventional carbon materials, activated charcoal and porous graphitic carbon (PGC), were investigated as sorbents to purify permethylated N-glycans derived from ribonuclease B and fetuin. The results confirmed the superior performance of CNPs over the other carbon materials. Additionally, our method was also employed to purify glycans released from human sera in different esophageal disease stages. The obtained data confirmed 16 and 18 structures in adenocarcinoma and Barret's sera with significantly different relative intensities versus disease-free sera. Comparing the performance of CNPs-based solid-phase purification method employed in this study to online purification suggested more than 97% recovery rate. The results of this study demonstrate that CNPs have the potential to be a better alternative to existing solid-phase purification sorbents.

SUBMITTER: Zhong J

PROVIDER: S-EPMC6294690 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature

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A carbon nanoparticles-based solid-phase purification method facilitating sensitive MALDI-MS analysis of permethylated N-glycans.

Zhong Jieqiang J Banazadeh Alireza A Peng Wenjing W Mechref Yehia Y

Electrophoresis 20180906 24

In recent decades, MALDI-MS has been extensively used for the analysis of glycans. However, native glycans usually have low ionization efficiency in MS, which hinders the direct analysis. Permethylation of glycans is a solution for this issue, but a significant amount of salt is introduced during this process, which can further suppress the MS signals. Thus, it is necessary to purify the glycans prior to MALDI-MS analysis. In this study, we developed a carbon nanoparticles-based solid-phase puri ...[more]

PMID: 30086189

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Project description:Sensitive glycomics analysis by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) is of great importance but significantly hampered by their low ionization efficiency and labile sialic acid moieties. Chemical derivatization offers a viable way to improve both the ionization efficiency and analytical sensitivity of the glycans in MS analysis by altering their hydrophobicity or charge property. Here we employed Girard's reagent T (GT) for on-target derivatization (GTOD) of reducing glycan under mild acid condition to form stable hydrazones at room temperature, allowing rapid and sensitive identification of neutral and sialylated glycans in positive-ion mode as only permanently positive charged molecular ions without multiple ion adducts by MALDI-TOF-MS. The MS signal intensities of lactose, sialylated N-glycans derived from bovine fetuin and neutral N-glycans derived from RNaseB and ovalbumin were boosted by 7.44, 9.13, 12.96 and 13.47 folds on average (n?=?3), respectively. More importantly, after GTOD strategy, unwanted desialylation of sialylated glycans during MS was suppressed. The detection limit of the assay is desirable since the nanogram of N-glycans derived from 0.16??g ovalbumin could be detected. The assay demonstrated good stability (RSD?2.95%, within 10 days), reliable reproducibility (RSD?=?2.96%, n?=?7) and a desirable linear dynamic range from 78?nmol/mL to 10??mol/mL. The strategy has been successfully applied to MS analysis of reducing glycans from human milks, neutral and sialylated O-, N-glycans from glycoproteins, and reducing glycans derived from glycosphingolipids, presenting neater [M]+ signals which allow detection of more low-abundance glycans and assignation of Neu5Ac vs. Neu5Gc or fucose vs. hexose in glycans due to the absence of the ambiguous interpretation from multiple peaks (ion adducts [M+Na]+ and [M+K]+). Moreover, the GTOD assay prevents desialylation during MALDI-TOF-MS profiling and enables distinct linkage-specific characterization of terminal sialic acids of N-glycans derived from human serum protein when combines with an esterification.

Dataset Information

A carbon nanoparticles-based solid-phase purification method facilitating sensitive MALDI-MS analysis of permethylated N-glycans.

Publications

A carbon nanoparticles-based solid-phase purification method facilitating sensitive MALDI-MS analysis of permethylated N-glycans.

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