Evidence map›Paper›PMID 34227319›Full record

ArticleSe pu = Chinese journal of chromatography2021

[Covalent organic framework functional materials and their applications in glycopeptide enrichment].

Qianying Sheng, Yang Zhou, Zhiquan Zhao, Yaohui Wang, Weicheng Li, Yanxiong Ke, Minbo Lan, Guangyan Qing, Xinmiao Liang

Open access · hybridAbstract read
In one paragraph

Article in Se pu = Chinese journal of chromatography, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 66% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 1 country.

Qianying ShengSchool of Chemistry and Molecular Engineering, East China University of Science and Technology, Shanghai 200237, China.
Yang ZhouSchool of Pharmacy, East China University of Science and Technology, Shanghai, 200237, China.
Zhiquan ZhaoSchool of Chemistry and Molecular Engineering, East China University of Science and Technology, Shanghai 200237, China.
Yaohui WangSchool of Chemistry and Molecular Engineering, East China University of Science and Technology, Shanghai 200237, China.
Weicheng LiSchool of Chemistry and Molecular Engineering, East China University of Science and Technology, Shanghai 200237, China.
Yanxiong KeSchool of Pharmacy, East China University of Science and Technology, Shanghai, 200237, China.
Minbo LanSchool of Chemistry and Molecular Engineering, East China University of Science and Technology, Shanghai 200237, China.
Guangyan QingDalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China.
Xinmiao LiangSchool of Pharmacy, East China University of Science and Technology, Shanghai, 200237, China.
East China University of Science and Technology · CNChinese Academy of Sciences · CNDalian Institute of Chemical Physics · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein glycosylation is among the most important post-translational modifications in living organisms and the research in the field of protein glycosylation continues to garner attention. Currently, the efficient separation and enrichment of glycoproteins and glycopeptides is the primary challenge of glycoproteomics research. The number of glycoproteins is small in complex biological samples. Moreover, the presence of highly-abundant, non-glycosylated, and modified peptides makes the detection of low-abundance glycopeptides more difficult. Therefore, efficient glycopeptide enrichment methods are required to improve the detection of these compounds. The development of highly selective glycopeptide enrichment tools is important to efficiently capture glycoproteins or glycopeptides at the molecular level. Compared with traditional glycopeptide-enriched materials, covalent organic framework materials have the advantages of large specific surface area and rich modification sites, thereby exhibiting great application potential in the field of glycopeptide enrichment. In this study, a novel covalent organic framework material (O-T-D-COFs) was prepared and applied for selective glycopeptide enrichment. We applied the solvothermal method, using 2,5-dimethoxy benzene-1,4-2 formaldehyde and 1,3,5-Tris(4-aminophenyl) benzene, to synthesize imino-based COFs. The Schiff base generated via copolymerization condensation reaction constitutes the framework of the material. Next, the synthesized intermediate material was oxidized to improve the enrichment performance of the material. The functional, specific glycopeptide-binding groups were modified on the COF channels and the structure of the material was characterized using scanning and transmission electron microscope, as well as infrared spectrum and solid-state nuclear magnetic resonance. The enrichment conditions comprised the loading and elution steps, including the optimization of the elution conditions. We could observe the clear profile of 32 glycopeptides derived from human serum immunoglobulin G (IgG) tryptic digests with a significantly improved signal-to-noise (

Indexed as

GlycopeptidesGlycosylationMetal-Organic FrameworksGlycoproteinsHumansHydrophobic and Hydrophilic InteractionsGlycopeptidesGlycoproteinsMetal-Organic Frameworkscovalent organic framework (COF) materialfunctional modificationglycopeptidesmass spectrometry (MS)selective enrichment

Identifiers

PMID34227319
PMCPMC9404058
OpenAlexW3179765479

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.