Evidence map›Paper›PMID 24236085›Full record

ArticlePloS one2013

Characterization of hydrophobic peptides in the presence of detergent by photoionization mass spectrometry.

Aïcha Bagag, Jean-Michel Jault, Nazha Sidahmed-Adrar, Matthieu Réfrégiers, Alexandre Giuliani, François Le Naour

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed, 1 pooled it
0.5field-weighted citation impact, top 37% of its field
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

16 citing papers in PubMed, 1 synthesis or guideline pooled it, 41 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
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  5. Article
  6. Article
  7. Peptide Analysis by Soft X-ray Atmospheric Pressure Photoionization Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2025
    Article
  8. Article
  9. Article
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  11. Article
  12. Article
  13. Article
  14. Overexpression of Cotton aFrontiers in plant science · 2019
    Article
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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

6 authors at 4 institutions in 2 countries.

Aïcha BagagInserm, U785, Villejuif, France ; Université Paris-Sud 11, Institut André Lwoff, Villejuif, France.
Jean-Michel Jault
Nazha Sidahmed-Adrar
Matthieu Réfrégiers
Alexandre Giuliani
François Le Naour
Synchrotron soleil · FRUniversité Paris-Sud · FRCommissariat à l'Énergie Atomique et aux Énergies Alternatives · FRInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The characterization of membrane proteins is still challenging. The major issue is the high hydrophobicity of membrane proteins that necessitates the use of detergents for their extraction and solubilization. The very poor compatibility of mass spectrometry with detergents remains a tremendous obstacle in studies of membrane proteins. Here, we investigated the potential of atmospheric pressure photoionization (APPI) for mass spectrometry study of membrane proteins. This work was focused on the tetraspanin CD9 and the multidrug transporter BmrA. A set of peptides from CD9, exhibiting a broad range of hydropathicity, was investigated using APPI as compared to electrospray ionization (ESI). Mass spectrometry experiments revealed that the most hydrophobic peptides were hardly ionized by ESI whereas all peptides, including the highly hydrophobic one that corresponds to the full sequence of the first transmembrane domain of CD9, were easily ionized by APPI. The native protein BmrA purified in the presence of the non-ionic detergent beta-D-dodecyl maltoside (DDM) was digested in-solution using trypsin. The resulting peptides were investigated by flow injection analysis of the mixture followed by mass spectrometry. Upon ESI, only detergent ions were detected and the ionic signals from the peptides were totally suppressed. In contrast, APPI allowed many peptides distributed along the sequence of the protein to be detected. Furthermore, the parent ion corresponding to the first transmembrane domain of the protein BmrA was detected under APPI conditions. Careful examination of the APPI mass spectrum revealed a-, b-, c- and y- fragment ions generated by in-source fragmentation. Those fragment ions allowed unambiguous structural characterization of the transmembrane domain. In conclusion, APPI-MS appears as a versatile method allowing the ionization and fragmentation of hydrophobic peptides in the presence of detergent.

Indexed as

Amino Acid SequenceATP-Binding Cassette TransportersDetergentsGlucosidesHumansHydrophobic and Hydrophilic InteractionsPeptide FragmentsSpectrometry, Mass, Electrospray IonizationTetraspanin 29ATP-Binding Cassette TransportersCD9 protein, humanDetergentsdodecyl maltosideGlucosidesPeptide FragmentsTetraspanin 29

Identifiers

PMID24236085
PMCPMC3827311
OpenAlexW2014690911

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.