Evidence map›Paper›PMID 40255129›Full record

ArticleRapid communications in mass spectrometry : RCM2025

Buffer 4-Ethylmorpholinium/Acetate: Exploring a New Alternative Buffer for Native Mass Spectrometry.

Darya Hadavi, Che Yee Ng, Yuandi Zhao, Anjusha Mathew, Ian G M Anthony, Berta Cillero-Pastor, Eva Cuypers, Tiffany Porta Siegel, Maarten Honing

Abstract read
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In one paragraph

Article in Rapid communications in mass spectrometry : RCM, 2025. 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. Review
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

9 authors.

Darya HadaviMaastricht Multi Modal Molecular Imaging (M4i) Institute, Division of Imaging Mass Spectrometry (IMS), Maastricht University, Maastricht, The Netherlands.
Che Yee NgMaastricht Multi Modal Molecular Imaging (M4i) Institute, Division of Imaging Mass Spectrometry (IMS), Maastricht University, Maastricht, The Netherlands.
Yuandi ZhaoMaastricht Multi Modal Molecular Imaging (M4i) Institute, Division of Imaging Mass Spectrometry (IMS), Maastricht University, Maastricht, The Netherlands.ORCID https://orcid.org/0000-0001-5376-140X
Anjusha MathewMaastricht Multi Modal Molecular Imaging (M4i) Institute, Division of Imaging Mass Spectrometry (IMS), Maastricht University, Maastricht, The Netherlands.
Ian G M AnthonyMaastricht Multi Modal Molecular Imaging (M4i) Institute, Division of Imaging Mass Spectrometry (IMS), Maastricht University, Maastricht, The Netherlands.
Berta Cillero-PastorMaastricht Multi Modal Molecular Imaging (M4i) Institute, Division of Imaging Mass Spectrometry (IMS), Maastricht University, Maastricht, The Netherlands.
Eva CuypersMaastricht Multi Modal Molecular Imaging (M4i) Institute, Division of Imaging Mass Spectrometry (IMS), Maastricht University, Maastricht, The Netherlands.
Tiffany Porta SiegelMaastricht Multi Modal Molecular Imaging (M4i) Institute, Division of Imaging Mass Spectrometry (IMS), Maastricht University, Maastricht, The Netherlands.
Maarten HoningMaastricht Multi Modal Molecular Imaging (M4i) Institute, Division of Imaging Mass Spectrometry (IMS), Maastricht University, Maastricht, The Netherlands.

Funding

DARTBAC NWA.1292.19.354Dutch Province of LimburgDutch Research Council
6 · The paper itself

Abstract

rationaleTo perform native mass spectrometry (MS) studies, there are a limited number of volatile and electrospray ionization (ESI)-MS compatible solutions, such as ammonium bicarbonate and ammonium acetate (AA). These solutions could induce the unfolding of proteins due to the formation of CO

methodsThe 4-ethylmorpholinium/acetate (4EM/A) buffer was compared to AA for the analysis of proteins and protein complexes with mass ranges from 5 to 103 kDa and isoelectric points (pI) between 3 and 11. The evaluations were conducted by comparing the native-MS profiles, CCS values, arrival time distributions (ATDs), and proteins bioactivities. The human cardiac troponin complex (cTn complex) and its subunit cardiac troponin T (cTnT) were analyzed as proof of the applicability of this buffer for challenging proteins and protein complexes.

results4EM/A led to lower charge states compared to AA, supporting the likelihood of preserving protein folding during nano-ESI and in a high vacuum environment of MS. Ion mobility measurements revealed that proteins in 4EM/A exhibit a lower degree of conformational variation compared to AA, suggesting enhanced conformational stability and potential retention of natural-like compactness. Additionally, testing the impact of 4EM/A on bioactivity, lysozyme showed increased biological activity in 4EM/A relative to AA, highlighting the buffer's potential for real-time assessment of protein interaction kinetics and bioactivity. The 4EM/A buffer enabled native-MS analysis of cTnT for the first time.

conclusionWe introduced 4EM/A, with pK

Indexed as

BuffersMorpholinesSpectrometry, Mass, Electrospray IonizationAcetatesAnimalsProtein ConformationProteinsAcetatesammonium acetateBuffersMorpholinesProteinscharge state distributionethylmorpholineion mobility spectrometrynative mass spectrometryprotein complexes

Identifiers

PMID40255129
PMCPMC12010238

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Registered trials

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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.