Assay for characterizing adsorption-properties of surfaces (APS).

LC-MS/MS based label-free quantification adsorption-dependent loss of molecules interaction of solubilized molecules with surfaces

Journal

Chemistry (Weinheim an der Bergstrasse, Germany)
ISSN: 1521-3765
Titre abrégé: Chemistry
Pays: Germany
ID NLM: 9513783

Informations de publication

Date de publication:
27 Aug 2024
Historique:
received: 09 08 2024
accepted: 26 08 2024
medline: 27 8 2024
pubmed: 27 8 2024
entrez: 27 8 2024
Statut: aheadofprint

Résumé

Analytes, from sample preparation, until entering an analytical instrument, are prone to adsorb to surfaces, driven by the chemical properties of the surface and the liquids they are dissolved in. This problem can be addressed with internal standards when a single or few known analytes are quantified that are usually not available in omics. However, minimal to no loss of analytes is the aim. Here, we present a novel assay for qualifying and quantifying interactions responsible for adsorption of molecules to surfaces (APS) by using LC-MS/MS-based differential quantitative analysis. To reflect a broad range of chemical interactions with surfaces, a reference mixture of thousands of tryptic peptides, with known compositions was selected, representing a variety of different chemical characteristics. The assay was tested by investigating the adsorption properties of several different vials with different surface chemistries. A significant number of hydrophobic peptides adsorbed to conventional polypropylene vials. In contrast, only few peptides adsorbed to polypropylene vials, assigned as low-protein-binding. The highest number of peptides adsorbed to glass vials driven by electrostatic interactions. In summary, the new assay is suitable to characterize adsorption properties of different surfaces and to approximate the loss of analytes during sample preparation.

Identifiants

pubmed: 39189660
doi: 10.1002/chem.202403000
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

e202403000

Informations de copyright

© 2024 Wiley‐VCH GmbH.

Auteurs

Bente Siebels (B)

University Medical Center Hamburg-Eppendorf, Section Mass Spectrometry and Proteomics, Martinistr. 52, 20251, Hamburg, GERMANY.

Manuela Moritz (M)

University Medical Center Hamburg-Eppendorf, Section Mass Spectrometry and Proteomics, GERMANY.

Diana Hübler (D)

Eppendorf AG, Devision Consumables, GERMANY.

Antonia Gocke (A)

University Medical Center Hamburg-Eppendorf, Section Mass Spectrometry and Proteomics, GERMANY.

Maria Riedner (M)

University of Hamburg, Technology Platform Mass Spectrometry, GERMANY.

Hannah Voß (H)

University Medical Center Hamburg-Eppendorf, Section Mass Spectrometry and Proteomics, GERMANY.

Hartmut Schlüter (H)

University Medical Center Hamburg-Eppendorf, Section Mass Spectrometry and Proteomics, Martinistr. 52, 20246, Hamburg, GERMANY.

Classifications MeSH