Development of nanomaterial enabling highly sensitive surface‐assisted laser desorption/ionization mass spectrometry peptide analysis. (21st February 2023)

• Record Type: Journal Article
• Authors: Cournut, Aline; Hosu, Ioana Silvia; Braud, Flavie; Moustiez, Paul; Coffinier, Yannick; Enjalbal, Christine; Bich, Claudia
• Is Part Of: Rapid communications in mass spectrometry. Volume 37:Number 8(2023)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2023-02-21
• Subjects: Mass spectrometry -- Periodicals; 543.65
• DOI: 10.1002/rcm.9476
• Languages: English
• ISSNs: 0951-4198

Abstract

Abstract : Rationale: 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. Methods: 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. Results: 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. Conclusions: 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.