Hydrophilic Mesoporous Silica Materials for Highly Specific Enrichment of N-Linked Glycopeptide

Sun, Nianrong; Wang, Jiawen; Yao, Jizong; Deng, Chunhui

doi:10.1021/acs.analchem.6b04054

Cited by 124 publications

(50 citation statements)

References 32 publications

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“…Retention of hydrophilic and charged glycopeptides or glycans on HILIC depends on partitioning, hydrogen bonding, dipole–dipole interactions as well as ionic interactions between the analytes and stationary phases . A series of HILIC stationary phases with diverse bonded functional groups were employed for the enrichment and separation of polar glyco‐compounds, including amide phase, diol phase, amino phase, zwitterionic phase, and so forth . In addition, various saccharide‐based stationary phases have also been developed and employed in the enrichment of glycopeptides and glycans, including click maltose, click chitooligosaccharide, and Sepharose .…”

Section: Introductionmentioning

confidence: 99%

Selective enrichment of N‐linked glycopeptides and glycans by using a dextran‐modified hydrophilic material

Chen

Ding

Sheng

et al. 2018

J of Separation Science

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Glycosylation analysis of proteins from biological sources utilizing mass spectrometry based approaches is challenging due to the relatively low abundance of glycopeptides, the structural diversity of glycans, and the coexisting matrices. In this study, a customized dextran-bonded silica-based stationary phase was introduced for selective enrichment of glycopeptides and glycans from complex biological samples. This material has exhibited superior selectivity and broader glycosylation site coverage over commercial Sepharose in glycoproteomic evaluation. Additionally, the glycomic analysis of fetuin, α -acid glycoprotein, and human serum N-glycome also indicated the relatively higher sensitivity, selectivity, and glycoform coverage of dextran-bonded silica than that of Sepharose and porous graphitized carbon. Therefore, the dextran-bonded silica is expected to make contributions in the fields of glycoproteomics and glycomics.

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Section: Introductionmentioning

confidence: 99%

Selective enrichment of N‐linked glycopeptides and glycans by using a dextran‐modified hydrophilic material

Chen

Ding

Sheng

et al. 2018

J of Separation Science

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Section: Nanomaterials In Glycoproteomicsmentioning

confidence: 99%

“…Other Zwitterionic Hydrophilic Nanomaterials : The other zwitterionic hydrophilic nanomaterials appeared in recent years mainly take IDA as functional zwitterionic group, which consists of two kinds of charges that are positive and negative. For example, IDA functionalized chitosan nanomaterials (CS@PGMA@IDA), IDA functionalized magnetic mesoporous nanomaterials (Fe 3 O 4 @mSiO 2 –IDA), as well as the IDA functionalized polymer monoliths (poly(GMA–EDMA–CuMPc–IDA), were respectively developed for glycopeptides capture. Different modification methods were adopted to graft IDA onto the surface of diverse substrates, one of which was chosen as an example to be displayed in Figure D.…”

Section: Nanomaterials In Glycoproteomicsmentioning

confidence: 99%

Nanomaterials in Proteomics

Sun

Shen

et al. 2019

Adv Funct Materials

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For a deep understanding of the human proteome, the first crucial step is always the effective separation of targeted proteins/peptides from complex samples. In mass spectrometry‐based proteomics, nanomaterials have emerged as a highly effective means to separate targeted proteins/peptides and increase their relative abundance, which is beneficial to conduct mass spectrometric analysis. In particular, nanomaterials with different specific functionalities have received great attention in ordinary proteomics, phosphoproteomics, and glycoproteomics, for which the easily recognizable characteristics of these proteomes take the primary responsibility, such as the hydrophobicity, phosphate groups, cis–diol structure, and hydrophilicity. This review mainly focuses on the recent design and preparation of nanomaterials with specific recognition ability, as well as their application in the aforementioned three types of proteomics.

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“…In addition, because the proportion of glycosylated peptides in protein enzymatic peptides is very low, there are still many limitations in directly analyzing them using MS. Moreover, the ionization efficiency of non‐glycopeptides is much higher than that of glycopeptides, and their presence leads to the inhibition of glycopeptide signals in complex systems by non‐glycopeptides . Therefore, it is difficult to directly determine glycopeptides by MS, which requires a method for isolating glycopeptides from complex biological samples.…”

Section: Introductionmentioning

confidence: 99%

“…Moreover, the ionization efficiency of non-glycopeptides is much higher than that of glycopeptides, and their presence leads to the inhibition of glycopeptide signals in complex systems by nonglycopeptides. [7][8][9] Therefore, it is difficult to directly determine glycopeptides by MS, which requires a method for isolating glycopeptides from complex biological samples.…”

Section: Introductionmentioning

confidence: 99%

Postsynthesis of zwitterionic hydrophilic composites for enhanced enrichment of N‐linked glycopeptides from human serum

Liu

Wang

Yan

et al. 2020

Rapid Comm Mass Spectrometry

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Rationale Glycosylation of proteins plays an important role in life activities, but the concentration of naturally occurring glycopeptides is usually relatively low, and glycosylation has microfacies heterogeneity, so direct mass spectrometry is not feasible. Therefore, selective enrichment of glycopeptides before mass spectrometry has turned into an urgent problem to be resolved. Methods Herein, the zwitterionic L‐cysteine functionalized hydrophilic graphene oxide composite (GO@PDA@MIL‐125‐NH2@Au@L‐Cys) was prepared via a postsynthetic method. The obtained material was used for glycopeptide enrichment. The enriched peptides were then detected using matrix‐assisted laser desorption ionization time‐of‐flight mass spectrometry (MALDI‐TOFMS) to demonstrate the enrichment performance of the material. Results In the actual enrichment process, GO@PDA@MIL‐125‐NH2@Au@L‐Cys nanomaterials exhibited high selectivity (1:1000), outstanding sensitivity (0.5 fmol), and excellent repeatability for the enrichment of glycopeptides. In addition, the proposed material showed good performance in the enrichment of glycopeptides from complex biosamples; 56 glycopeptides were detected from 2 μL of human serum using MALDI‐TOFMS. Conclusions The experimental results showed that GO@PDA@MIL‐125‐NH2@Au@L‐Cys exhibited excellent performance on glycopeptide analysis. It has great potential in the enrichment of glycopeptides and provides new ideas for synthetic materials with better enrichment properties in the future.

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Hydrophilic Mesoporous Silica Materials for Highly Specific Enrichment of N-Linked Glycopeptide

Cited by 124 publications

References 32 publications

Selective enrichment of N‐linked glycopeptides and glycans by using a dextran‐modified hydrophilic material

Selective enrichment of N‐linked glycopeptides and glycans by using a dextran‐modified hydrophilic material

Nanomaterials in Proteomics

Postsynthesis of zwitterionic hydrophilic composites for enhanced enrichment of N‐linked glycopeptides from human serum

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