Highly specific enrichment of N-linked glycopeptides based on hydrazide functionalized soluble nanopolymers

Zhang, Lijuan; Jiang, Hucong; Yao, Jun; Wang, Yali; Fang, Changming; Yang, Pengyuan; Lu, Haojie

doi:10.1039/c3cc47347c

Cited by 49 publications

(24 citation statements)

References 24 publications

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“…175 N‐glycopeptides corresponding to 63 glycoproteins were identified from 20 µL of colorectal cancer patient serum in three runs, exhibiting 69.6% and 80.9% of captured specificities toward glycopeptides and glycoproteins, respectively. Also more other hydrazide‐based nanomaterials were explored by using different routes for various hydrazide source . An interesting pH‐responsive polymer with the ability of reversible self‐assembly and phase separation in aqueous solution was reported by Bai's group, which was prepared by copolymerization of poly‐(acrylic acid) and hydrazide, and therefore denoted as poly‐(AA‐co‐hydrazide).…”

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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Section: Nanomaterials In Glycoproteomicsmentioning

confidence: 99%

Nanomaterials in Proteomics

Sun

Shen

et al. 2019

Adv Funct Materials

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“…e) Structure of Fe 3 O 4 @poly(methacrylic hydrazide) core–shell magnetic nanocomposites . f) Structure of hydrazide‐functionalized poly(amido amine) dendrimer . The introduction of functional polymer as the polymeric core or shell provides abundant binding sites (i.e., boronate or hydrazine) for saccharides or glycans, leading to much stronger affinity and higher enrichment selectivity toward GPs.…”

Section: Polymeric Materials For Glycopeptide (Gp) Enrichmentmentioning

confidence: 99%

“…In contrast, Lu and co‐workers synthesized a soluble nanopolymer (Figure f) using poly(amido amine) (PAMAM) as the soft supporting matrix and then grafted hydrazide groups through a two‐step derivatization reaction. Excellent solubility and high structural homogeneity of the soluble nanopolymer promoted the complete contact between the material and the GPs in the reaction solution, considerably improving the sensitivity toward GPs.…”

Section: Polymeric Materials For Glycopeptide (Gp) Enrichmentmentioning

confidence: 99%

New Opportunities and Challenges of Smart Polymers in Post‐Translational Modification Proteomics

et al. 2017

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Protein post-translational modifications (PTMs), which denote covalent additions of various functional groups (e.g., phosphate, glycan, methyl, or ubiquitin) to proteins, significantly increase protein complexity and diversity. PTMs play crucial roles in the regulation of protein functions and numerous cellular processes. However, in a living organism, native PTM proteins are typically present at substoichiometric levels, considerably impeding mass-spectrometry-based analyses and identification. Over the past decade, the demand for in-depth PTM proteomics studies has spawned a variety of selective affinity materials capable of capturing trace amounts of PTM peptides from highly complex biosamples. However, novel design ideas or strategies are urgently required for fulfilling the increasingly complex and accurate requirements of PTM proteomics analysis, which can hardly be met by using conventional enrichment materials. Considering two typical types of protein PTMs, phosphorylation and glycosylation, an overview of polymeric enrichment materials is provided here, with an emphasis on the superiority of smart-polymer-based materials that can function in intelligent modes. Moreover, some smart separation materials are introduced to demonstrate the enticing prospects and the challenges of smart polymers applied in PTM proteomics.

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“…The common enrichment strategies based on glycan-specific recognition or glycan physicochemical properties for glycosylated proteins/peptides, including lectin affinity, 9 − 12 hydrazide chemistry, 13 − 15 boronic acid chemistry, 16 − 21 and hydrophilic interaction liquid chromatography (HILIC), 22 − 25 have been developed. Among them, HILIC has aroused much attention for glycopeptides enrichment by utilizing the strong hydrophilicity of the glycopeptides and HILIC materials, due to its broad glycan specificity, excellent reproducibility, and good MS compatibility.…”

Section: Introductionmentioning

confidence: 99%

Maltose-Functionalized Hydrophilic Magnetic Nanoparticles with Polymer Brushes for Highly Selective Enrichment of N-Linked Glycopeptides

Liang

Shen

et al. 2018

ACS Omega

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Efficient enrichment glycoproteins/glycopeptides from complex biological solutions are very important in the biomedical sciences, in particular biomarker research. In this work, the high hydrophilic polyethylenimine conjugated polymaltose polymer brushes functionalized magnetic Fe3O4 nanoparticles (NPs) denoted as Fe3O4–PEI–pMaltose were designed and synthesized via a simple two-step modification. The obtained superhydrophilic Fe3O4–PEI–pMaltose NPs displayed outstanding advantages in the enrichment of N-linked glycopeptides, including high selectivity (1:100, mass ratios of HRP and bovine serum albumin (BSA) digest), low detection limit (10 fmol), large binding capacity (200 mg/g), and high enrichment recovery (above 85%). The above-mentioned excellent performance of novel Fe3O4–PEI–pMaltose NPs was attributed to graft of maltose polymer brushes and efficient assembly strategy. Moreover, Fe3O4–PEI–pMaltose NPs were further utilized to selectively enrich glycopeptides from human renal mesangial cell (HRMC, 200 μg) tryptic digest, and 449 N-linked glycopeptides, representing 323 different glycoproteins and 476 glycosylation sites, were identified. It was expected that the as-synthesized Fe3O4–PEI–pMaltose NPs, possessing excellent performance (high binding capacity, good selectivity, low detection limit, high enrichment recovery, and easy magnetic separation) coupled to a facile preparation procedure, have a huge potential in N-glycosylation proteome analysis of complex biological samples.

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Highly specific enrichment of N-linked glycopeptides based on hydrazide functionalized soluble nanopolymers

Abstract: In this work, for the first time, hydrazide functionalized PAMAM was designed and synthesized for efficient and selective enrichment of N-linked glycopeptides from complex biological samples using FASP (filter-aided sample preparation) mode.

Cited by 49 publications

References 24 publications

Nanomaterials in Proteomics

Nanomaterials in Proteomics

New Opportunities and Challenges of Smart Polymers in Post‐Translational Modification Proteomics

Maltose-Functionalized Hydrophilic Magnetic Nanoparticles with Polymer Brushes for Highly Selective Enrichment of N-Linked Glycopeptides

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