Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Evaluation of absorbent cotton for glycopeptide enrichment

ABSTRACT: This study introduced the use of cotton in 200µL tips, namely cotton HILIC as a convenient tool for enriching large-scale glycopeptides before MS analysis in this study. The optimal loading buffer for cotton HILIC was investigated by using mouse brain as a complex test sample. Subsequently, the performance of cotton HILIC was evaluated by comparing with other two commercial enrichment approaches, venusil HILIC and Oasis MAX in both mouse brain and seminal plasma. Moreover, capacity and recovery rate were evaluated using different milligram of cotton in 200µL tips. Thus, a simple, convenient, and cost-friendly cotton HILIC method was proposed to achieve highly selective intact glycopeptide profiling.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Brain

SUBMITTER: Miaomiao Xin

LAB HEAD: Shisheng Sun

PROVIDER: PXD035078 | Pride | 2023-03-04

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	5mgcotton_48oug_XT1_you.raw	Raw
	5mgcotton_48oug_XT1_you_result.xlsx	Xlsx
	5mgcotton_48oug_XT2_you.raw	Raw
	5mgcotton_48oug_XT2_you_result.xlsx	Xlsx
	5mgcotton_48oug_XT3_you.raw	Raw

Items per page:

1 - 5 of 53

Similar Datasets

Structural Interpretation of Glycosite-specific N-Glycans Using Tandem Mass Spectrometry

Project description:In this project we developed a new algorithm termed StrucGP, for large-scale interpretation of N-glycan structures on intact glycopeptides from tandem mass spectrometry data. StrucGP is able to reveal the glycan structure heterogeneity for individual glycosites. The StrucGP also has high performance in distinguishing various structure isoforms and identifying new and rare glycan structures from complex samples.

2021-07-07 | PXD025859 | Pride

Glycoproteomic analysis of Fut8 knock out/wild type mouse brain, Human IgG and Human Serum.

Project description:In this study, we provide a simple and straightforward method to distinguish core-fucosylated glycans from antenna-fucosylated glycans by systematically evaluating the extent of fucose migration based on the feature Y ions by using Fut8 knockout (Fut8−/−) mouse brain under HCD energy of 20%. The method was further evaluated by multiple different approaches including validation by standard glycopeptides, evaluation in silico, comparison under the lower energy (15%), and applied to analyze core-fucosylated glycans in wide-type (Fut8+/+) mouse brain.

2022-11-14 | PXD035158 | Pride

Precision Characterization of Site-specific O-Acetylated Sialic Acids on N-Glycoproteins

Project description:O-Acetylation is a common modification of sialic acid, playing a significant role in glycoprotein stability, immune response, and cell development. The lack of efficient methods for direct analysis of O-acetylated sialoglycopeptides (O-AcSGPs) made the majority of identified O-acetylated sialic acids (O-AcSia) till now had no glycosite/glycoprotein information. Herein, we introduced a new workflow for precise interpretation of O-AcSGPs with probability estimation by recognizing the characteristic B and Y ions of O-AcSias.

2023-01-13 | PXD037161 | Pride

Hydrophilic interaction liquid chromatography contributes to integrated N-glycoproteomics analysis of human saliva for lung cancer

Project description:We aimed to in-depth characterize and quantify salivary N-glycoproteomics. HILIC enrichment and LC-MS/MS were combined to investigate salivary glycosylation both at deglycopeptides level and glycopepeptides level, and alterations in site-specific glycoforms for human saliva were detected between lung cancer patients and healthy subjects. Firstly, intact glycopeptides were enriched from human saliva through using HILIC. Obtained intact glycopeptides were characterized by LC-MS/MS directly. Furthermore, the glycosylation sites were fully identified by LC-MS/MS followed by incubating with PNGase F. The developed workflow was applied to compare N-glycosites and intact N-glycopeptides in lung cancer group and healthy control group. Dysregulated N-glycosites as well as site-specific glycoforms were confidently observed in lung cancer and their potential value in clinical applications will be discussed.

2023-02-08 | PXD030670 | Pride

A Fully Automated Enrichment and Separation System for Highly-reproducible and In-depth Analysis of Intact Glycopeptide

Project description:A fully automated HILIC-based enrichment and separation system for glycopeptide (AutoGP), which needs no sample collection, was developed in this study.

2024-05-06 | PXD050391 | Pride

Analysing the glycoproteome of Burkholderia multivorans following knockdown of glycosylation using CRISPR interference

Project description:To interrogate the glycoproteome following knockdown of pglL and subsequent knockdown of glycosylation in Burkholderia multivorans through Zwitterionic Hydrophilic Interaction Liquid Chromatography (ZIC-HILIC) glycopeptide enrichment

2023-03-20 | PXD037777 | Pride

Analysing the glycoproteome of Burkholderia diffusa following knockdown of glycosylation using CRISPR interference

Project description:To interrogate the glycoproteome following knockdown of pglL and subsequent knockdown of glycosylation in Burkholderia diffusa through Zwitterionic Hydrophilic Interaction Liquid Chromatography (ZIC-HILIC) glycopeptide enrichment

2023-03-20 | PXD037750 | Pride

Comparison of Intact Glycopeptide Enrichment Methods Using Strong Anion Exchange and Hydrophilic Interaction Liquid Chromatography

Project description:Heterogeneity of protein glycosylation poses great challenge for analysis that is key to un-puzzle systems glycobiology in diseases. Resolving this conundrum requires global enrichment of glycopeptides for identification and quantitation. To this aim, hydrophilic interaction chromatography (HILIC) has been proved to be an effective approach to enrich N-linked glycopeptides (N-glycopeptides). However, its effectiveness to enrich O-linked glycopeptides (O-glycopeptides) and isobaric labelled glycopeptides remains unclear. Here, we studied three different cartridges in HILIC mode. It was found that removal of N-glycosylation prior to enrichment improved identification of O-glycopeptides. It was noted that increased yield and number of glycosylation identification were seen when using cartridges having materials for strong anion exchange (SAX) chromatography. Remarkably, O-glycopeptides were found to be selectively enriched by HILIC with further improved enrichment being seen when Retain AX cartridge being used. Of particular note, isobaric labelled glycopeptides could be readily enriched by SAX cartridges in HILIC mode to enable quantitative glycoproteomics. It is anticipated that the use of SAX cartridges will facilitate broad applications of qualitative and quantitative glycoproteomics in diseases.

2017-10-19 | PXD005145 | Pride

Analysing the glycoproteome of Burkholderia cenocepacia following knockdown of glycosylation using CRISPR interference

Project description:To interrogate the glycoproteome following knockdown of pglL and subsequent knockdown of glycosylation in Burkholderia cenocepacia through Zwitterionic Hydrophilic Interaction Liquid Chromatography (ZIC-HILIC) glycopeptide enrichment. Using a pglL (BCAL0960)-targeting guide, and a non-target guide.

2023-03-20 | PXD037778 | Pride

Analysing the glycoproteome of Burkholderia thailandensis following knockdown of glycosylation using CRISPR interference

Project description:To interrogate the glycoproteome following knockdown of pglL and subsequent knockdown of glycosylation in Burkholderia thailandensis through Zwitterionic Hydrophilic Interaction Liquid Chromatography (ZIC-HILIC) glycopeptide enrichment. Using a pglL (BTH_I0650)-targeting guide, and a non-target guide.

2023-03-20 | PXD037773 | Pride