One-step functionalization of magnetic nanoparticles with 4-mercaptophenylboronic acid for a highly efficient analysis of N-glycopeptides

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

doi:10.1039/c7nr04206j

Cited by 50 publications

(25 citation statements)

References 33 publications

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“…The binding capacity of GO@MPBA for glycoproteins was 1288.8, 1144.1, 592.1, and 392.4 mg g −1 for OVA, Ig G, Trf, and HRP, respectively. Moreover, the MPBA was smartly immobilized on magnetic nanoparticles by the direct formation of FeS bond (Fe 3 O 4 –MPBA, Figure A) . Compared to the recent conventional ones, it can be regarded as the simplest synthetic process.…”

Section: Nanomaterials In Glycoproteomicsmentioning

confidence: 99%

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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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Section: Nanomaterials In Glycoproteomicsmentioning

confidence: 99%

Section: Nanomaterials In Glycoproteomicsmentioning

confidence: 99%

Nanomaterials in Proteomics

Sun

Shen

et al. 2019

Adv Funct Materials

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“…The captured peptides were specifically eluted and analyzed by MALDI-TOF MS. All the detailed glycan substructures were determined according to a previous report of glycopeptides list. [34][35][36][37][38] The selectivity of glycopeptides enrichment by poly(GMA-EDMA-CoPcTc) monolith was first evaluated using IgG digests. Figure 2 shows the MS spectra of IgG digests before and after enrichment by poly(GMA-EDMA) and poly(GMA-EDMA-CoPcTc) monoliths, respectively.…”

Section: Selectivity Of Poly(gma-edma-copctc) Monolith For Glycopeptimentioning

confidence: 99%

Cobalt Phthalocyanine Tetracarboxylic Acid Functionalized Polymer Monolith for Selective Enrichment of Glycopeptides and Glycans

et al. 2018

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In this study, poly(glycidyl methacrylate-ethyleneglycol dimethacrylate) monolith functionalized with cobalt phthalocyanine tetracarboxylic acid is prepared. The polymer monolithic material is used for glycopeptides enrichment coupled with MALDI-TOF MS. By taking advantage of cobalt phthalocyanine including hydrogen bonds between isoindole subunits of phthalocyanine and glycans, coordination interaction between cobalt and glycopeptides, the monolithic material is successfully applied to the enrichment of glycopeptides efficiently and selectively. With IgG and horse radish peroxidase as the model glycoproteins, 28 and 17 glycopeptides could be identified respectively after enrichment with the monolith, only four and three glycopeptides could be obtained for direct analysis. The monolith is also employed to the digests mixture of BSA and IgG (50:1, m/m), indicating the high enrichment selectivity of glycopeptides even in the presence of a large interference ratio. The detection limit is determined to be 6.7 fmol, implying that the present method had great potential for trace sample analysis. In addition, the monolith was successfully applied to the enrichment of N-linked glycans in human serum samples, demonstrating its great potential for the analysis of glycoproteins.

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Section: Introductionmentioning

confidence: 99%

“…Currently, using the unique chemical properties of the sugar chain of glycoproteins, some methods have been implemented to recognize glycopeptides, such as lectin chromatography, 10 volume exclusion chromatography, 11,12 hydrophilic interaction liquid chromatography (HILIC), [13][14][15][16] hydrazide chemistry, 17,18 and boronic acid chemistry. [19][20][21][22] Each method has its own merits and demerits. Lectin chromatography is simple in operation and mature in technology, while the disadvantage is that a lectin can enrich only a specific structure of glycoprotein or glycopeptide; for example, the most common lectin is concanavalin A (ConA), which is mainly used for the enrichment of high mannose-type N-glycoproteins, and has weak binding ability to dual-antenna sugar chains, but for three-or four-antenna sugar chains, it has no enrichment effect.…”

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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One-step functionalization of magnetic nanoparticles with 4-mercaptophenylboronic acid for a highly efficient analysis of N-glycopeptides

Cited by 50 publications

References 33 publications

Nanomaterials in Proteomics

Nanomaterials in Proteomics

Cobalt Phthalocyanine Tetracarboxylic Acid Functionalized Polymer Monolith for Selective Enrichment of Glycopeptides and Glycans

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

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