Evidence map›Paper›PMID 39189660›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2024

Assay for Characterizing Adsorption-Properties of Surfaces (APS).

Bente Siebels, Manuela Moritz, Diana Hübler, Antonia Gocke, Maria Riedner, Hannah Voß, Hartmut Schlüter

Abstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Article
  2. Assay for Characterizing Adsorption-Properties of Surfaces (APS).Chemistry (Weinheim an der Bergstrasse, Germany) · 2024
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Bente SiebelsSection Mass Spectrometry and Proteomics, University Medical Center Hamburg-Eppendorf, Martininstr. 52, Hamburg, 20246, Germany.ORCID https://orcid.org/0000-0001-9183-0381
Manuela MoritzSection Mass Spectrometry and Proteomics, University Medical Center Hamburg-Eppendorf, Martininstr. 52, Hamburg, 20246, Germany.ORCID https://orcid.org/0000-0002-8537-7493
Diana HüblerEppendorf SE, Barkhausenweg 1, Hamburg, 22339, Germany.ORCID https://orcid.org/0000-0002-4129-8398
Antonia GockeSection Mass Spectrometry and Proteomics, University Medical Center Hamburg-Eppendorf, Martininstr. 52, Hamburg, 20246, Germany.ORCID https://orcid.org/0009-0007-5828-6637
Maria RiednerTechnology Platform Mass Spectrometry, University Administration, University of Hamburg, Mittelweg 177, Hamburg, 20148, Germany.ORCID https://orcid.org/0000-0003-4421-998X
Hannah VoßSection Mass Spectrometry and Proteomics, University Medical Center Hamburg-Eppendorf, Martininstr. 52, Hamburg, 20246, Germany.
Hartmut SchlüterSection Mass Spectrometry and Proteomics, University Medical Center Hamburg-Eppendorf, Martininstr. 52, Hamburg, 20246, Germany.ORCID https://orcid.org/0000-0002-9358-7036

Funding

Deutsche Forschungsgemeinschaft INST 152/837-1Deutsche Forschungsgemeinschaft INST 152/947-1 FUGGDeutsche Forschungsgemeinschaft INST 337/15-1Deutsche Forschungsgemeinschaft INST 337/16-1
6 · The paper itself

Abstract

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.

Indexed as

Hydrophobic and Hydrophilic InteractionsPeptidesSurface PropertiesTandem Mass SpectrometryAdsorptionChromatography, LiquidPolypropylenesStatic ElectricityPeptidesPolypropylenesAdsorption-dependent loss of moleculesInteraction of solubilized molecules with surfacesLC–MS/MS based label-free quantification

Identifiers

PMID39189660
PMCPMC11618038

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.