Preparation of high-efficiency titanium ion immobilized magnetic graphite nitride nanocomposite for phosphopeptide enrichment.
Graphite nitride
Magnetic
Mass spectrum
Phosphopeptide enrichment
Titanium ion
Journal
Analytica chimica acta
ISSN: 1873-4324
Titre abrégé: Anal Chim Acta
Pays: Netherlands
ID NLM: 0370534
Informations de publication
Date de publication:
01 Dec 2023
01 Dec 2023
Historique:
received:
14
07
2023
revised:
25
10
2023
accepted:
26
10
2023
medline:
20
11
2023
pubmed:
18
11
2023
entrez:
17
11
2023
Statut:
ppublish
Résumé
Protein phosphorylation has been implicated in life processes including molecular interaction, protein structure transformation, and malignant disease. An in-depth study of protein phosphorylation may provide vital information for the discovery of early biomarkers. Mass spectrometry (MS)-based techniques have become an important method for phosphopeptide identification. Nevertheless, direct detection remains challenging because of the low ionization efficiency of phosphopeptides and serious interference from non-phosphopeptides. There is a great need for an efficient enrichment strategy to analyze protein phosphorylation prior to MS analysis. In this study, a novel nanocomposite was prepared by introducing titanium ions into two-dimensional magnetic graphite nitride. The nanocomposite was combined with immobilized metal ion affinity chromatography (IMAC) and anion-exchange chromatography mechanisms for phosphoproteome research. The nanocomposite had the advantages of a large specific surface (412.9 m We successfully designed and developed an efficient analysis platform for phosphopeptides, which includes protein digestion, phosphopeptide enrichment, and MS detection. The MS-based enrichment platform was further used to analyze phosphopeptides from complicated bio-samples. This work paves the way for the design and preparation of graphite nitride-based IMAC materials for phosphoproteome analysis.
Sections du résumé
BACKGROUND
BACKGROUND
Protein phosphorylation has been implicated in life processes including molecular interaction, protein structure transformation, and malignant disease. An in-depth study of protein phosphorylation may provide vital information for the discovery of early biomarkers. Mass spectrometry (MS)-based techniques have become an important method for phosphopeptide identification. Nevertheless, direct detection remains challenging because of the low ionization efficiency of phosphopeptides and serious interference from non-phosphopeptides. There is a great need for an efficient enrichment strategy to analyze protein phosphorylation prior to MS analysis.
RESULTS
RESULTS
In this study, a novel nanocomposite was prepared by introducing titanium ions into two-dimensional magnetic graphite nitride. The nanocomposite was combined with immobilized metal ion affinity chromatography (IMAC) and anion-exchange chromatography mechanisms for phosphoproteome research. The nanocomposite had the advantages of a large specific surface (412.9 m
SIGNIFICANCE
CONCLUSIONS
We successfully designed and developed an efficient analysis platform for phosphopeptides, which includes protein digestion, phosphopeptide enrichment, and MS detection. The MS-based enrichment platform was further used to analyze phosphopeptides from complicated bio-samples. This work paves the way for the design and preparation of graphite nitride-based IMAC materials for phosphoproteome analysis.
Identifiants
pubmed: 37977792
pii: S0003-2670(23)01195-9
doi: 10.1016/j.aca.2023.341974
pii:
doi:
Substances chimiques
Titanium
D1JT611TNE
Phosphopeptides
0
Graphite
7782-42-5
Caseins
0
Ions
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
341974Informations de copyright
Copyright © 2023 Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.