Development of nanomaterial enabling highly sensitive surface-assisted laser desorption/ionization mass spectrometry peptide analysis.
Journal
Rapid communications in mass spectrometry : RCM
ISSN: 1097-0231
Titre abrégé: Rapid Commun Mass Spectrom
Pays: England
ID NLM: 8802365
Informations de publication
Date de publication:
30 Apr 2023
30 Apr 2023
Historique:
revised:
14
01
2023
received:
14
12
2022
accepted:
18
01
2023
pubmed:
20
1
2023
medline:
16
3
2023
entrez:
19
1
2023
Statut:
ppublish
Résumé
Surface-assisted laser desorption/ionization mass spectrometry (SALDI-MS) is an approach derived from matrix-assisted laser desorption/ionization (MALDI)-MS which overcomes the drawbacks associated with the use of organic matrices required to co-crystallize with the analytes. Indeed, nanomaterials commonly used in SALDI-MS as inert surfaces to promote desorption/ionization (D/I) ensure straightforward direct deposition of samples while providing mass spectra with ions only related to the compound of interest. The objective of this study was to develop a novel SALDI-MS approach based on steel plates that are surfaces very rapidly and easily tuned to perform the most efficient peptide detection as possible. To compare the SALDI efficacy of such metal substrates, D/I efficiency and deposit homogeneity were evaluated according to steel plate fabrication processes. The studied surfaces were nanostructured steel plates that were chemically modified by perfluorosilane and textured according to different frequencies and laser writing powers. The capacity of each tested 100 surfaces was demonstrated by comparative analyses of a mixture of standard peptides (m/z 600-3000) performed with a MALDI-TOF instrument enabling MALDI, SALDI and imaging experiments. A peptide mix was used to screen the different surfaces depending on their D/I efficiency and their ability to ensure homogeneous deposit of the samples. For that purpose, deposition homogeneity was visualized owing to reconstructed ionic images from all protonated or sodiated ions of the 10 peptides constituting the standard mix. Seven surfaces were then selected satisfying the required D/I efficiency and deposit homogeneity criteria. Results obtained with these optimal surfaces were then compared with those recorded by MALDI-MS analyses used as references.
Substances chimiques
Peptides
0
Ions
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e9476Subventions
Organisme : Agence Nationale de la Recherche
ID : ANR NanoIntra ANR-19-CE09-0030
Organisme : Agence Nationale de la Recherche
ID : ANR-11-EQUIPEX-0025
Organisme : Centre National de la Recherche Scientifique (CNRS)
Organisme : University of Lille
Organisme : University of Montpellier
Organisme : RENATECH
Informations de copyright
© 2023 The Authors. Rapid Communications in Mass Spectrometry published by John Wiley & Sons Ltd.
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