Evidence map›Paper›PMID 18083584›Full record

ArticleJournal of the American Society for Mass Spectrometry2008

Which electrospray-based ionization method best reflects protein-ligand interactions found in solution? a comparison of ESI, nanoESI, and ESSI for the determination of dissociation constants with mass spectrometry.

Matthias Conradin Jecklin, David Touboul, Cédric Bovet, Arno Wortmann, Renato Zenobi

Erratum issuedOpen access · greenAbstract readComparative Study
PubMed Publisher
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

34 citing papers in PubMed, 105 citations in OpenAlex.

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  4. Norovirus-glycan interactions - how strong are they really?Biochemical Society transactions · 2022
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  5. Article
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  7. Protein-Ligand Affinity Determinations Using Covalent Labeling-Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2020
    Article
  8. Article
  9. Article
  10. Quantification of Protein-Ligand Interactions by Laser Electrospray Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2018
    Article
  11. Article
  12. Article
  13. On the preservation of non-covalent protein complexes during electrospray ionization.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2016
    Article
  14. Article
  15. Article
  16. Article
  17. Article
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4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Matthias Conradin JecklinDepartment of Chemistry and Applied Biosciences, ETH Zurich, Zurich, Switzerland.
David Touboul
Cédric Bovet
Arno Wortmann
Renato Zenobi
ETH Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We present a comparison of three different electrospray-based ionization techniques for the investigation of noncovalent complexes with mass spectrometry. The features and characteristics of standard electrospray ionization (ESI), chip-based nanoESI, and electrosonic spray ionization (ESSI) mounted onto a hybrid quadrupole time-of-flight mass spectrometer were compared in their performance to determine the dissociation constant (KD) of the model system hen egg white lysozyme (HEWL) binding to N,N',N''-triacetylchitotriose (NAG3). The best KD value compared with solution data were found for ESSI, 19.4 +/- 3.6 microM. Then, we determined the KDs of the two nucleotide binding sites of adenylate kinase (AK), where we obtained KDs of 2.2 +/- 0.8 microM for the first and 19.5 +/- 8.0 microM for the second binding site using ESSI. We found a weak charge state dependence of the KD for both protein-ligand systems, where for all ionization techniques the KD value decreases with increasing charge state. We demonstrate that ESSI is very gentle and insensitive to instrumental parameters, and the KD obtained is in good agreement with solution phase results from the literature. In addition, we tried to determine the KD for the lymphocyte-specific kinase LCK binding to a kinase inhibitor using nanoESI due to the very low amount of sample available. In this case, we found KD values with a strong charge state dependence, which were in no case close to literature values for solution phase.

Indexed as

LigandsAdenosine DiphosphateAdenylate KinaseAnimalsChickensHumansLymphocyte Specific Protein Tyrosine Kinase p56(lck)MuramidaseProtein BindingProtein Kinase InhibitorsProteinsSpectrometry, Mass, Electrospray IonizationTitrimetryTrisaccharidesAdenosine DiphosphateAdenylate Kinasehen egg lysozymeLigandsLymphocyte Specific Protein Tyrosine Kinase p56(lck)MuramidaseN,N',N''-triacetylchitotrioseProtein Kinase InhibitorsProteinsTrisaccharides

Identifiers

PMID18083584
OpenAlexW2062488259

What OpenQuestion holds

Textmetadata
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.