Evidence map›Paper›PMID 35076780›Full record

ArticleAmino acids2022

Identification of bacterial lipo-amino acids: origin of regenerated fatty acid carboxylate from dissociation of lipo-glutamate anion.

Amandine Hueber, Yves Gimbert, Geoffrey Langevin, Jean-Marie Galano, Alexandre Guy, Thierry Durand, Nicolas Cenac, Justine Bertrand-Michel, Jean-Claude Tabet

Open access · hybridAbstract read
In one paragraph

Article in Amino acids, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.4field-weighted citation impact, top 46% 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

1 citing paper in PubMed, 4 citations in OpenAlex.

  1. 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

9 authors at 3 institutions in 2 countries.

Amandine HueberMetaboHUB-MetaToul, National Infrastructure of Metabolomics and Fluxomics, 31077, Toulouse, France.
Yves GimbertSorbonne Université, CNRS, Institut Parisien de Chimie Moléculaire (UMR 8232), 4 place Jussieu, 75005, Paris, France.
Geoffrey LangevinInstitut Des Biomolécules Max Mousseron, UMR 5247, CNRS, Université de Montpellier-ENSCM, 34093, Montpellier, France.
Jean-Marie GalanoInstitut Des Biomolécules Max Mousseron, UMR 5247, CNRS, Université de Montpellier-ENSCM, 34093, Montpellier, France.
Alexandre GuyInstitut Des Biomolécules Max Mousseron, UMR 5247, CNRS, Université de Montpellier-ENSCM, 34093, Montpellier, France.
Thierry DurandInstitut Des Biomolécules Max Mousseron, UMR 5247, CNRS, Université de Montpellier-ENSCM, 34093, Montpellier, France.
Nicolas CenacIRSD, Université de Toulouse, INSERM, INRA, INPENVT, Université de Toulouse, 3 Paul Sabatier, 31024, Toulouse, France.
Justine Bertrand-MichelMetaboHUB-MetaToul, National Infrastructure of Metabolomics and Fluxomics, 31077, Toulouse, France. justine.bertrand-michel@inserm.fr.ORCID http://orcid.org/0000-0001-9815-1517
Jean-Claude TabetMetaboHUB-MetaToul, National Infrastructure of Metabolomics and Fluxomics, 31077, Toulouse, France.
École Nationale Supérieure de Chimie de Montpellier · FRUniversité Toulouse III - Paul Sabatier · FRCentre National de la Recherche Scientifique · FR

Funding

Inserm PhD GrantRégion Occitanie PhD Grant
6 · The paper itself

Abstract

The identification of bacterial metabolites produced by the microbiota is a key point to understand its role in human health. Among them, lipo-amino acids (LpAA), which are able to cross the epithelial barrier and to act on the host, are poorly identified. Structural elucidation of few of them was performed by high-resolution tandem mass spectrometry based on electrospray combined with selective ion dissociations reach by collision-induced dissociation (CID). The negative ions were used for their advantages of yielding only few fragment ions sufficient to specify each part of LpAA with sensitivity. To find specific processes that help structural assignment, the negative ion dissociations have been scrutinized for an LpAA: the N-palmitoyl acyl group linked to glutamic acid (C16Glu). The singular behavior of [C16Glu-H]¯ towards CID showed tenth product ions, eight were described by expected fragment ions. In contrast, instead of the expected product ions due to CONH-CH bond cleavage, an abundant complementary dehydrated glutamic acid and fatty acid anion pair were observed. Specific to glutamic moiety, they were formed by a stepwise dissociation via molecular isomerization through ion-dipole formation prior to dissociation. This complex dissociated by partner splitting either directly or after inter-partner proton transfer. By this pathway, surprising regeneration of deprotonated fatty acid takes place. Such regeneration is comparable to that occurred from dissociation to peptides containing acid amino-acid. Modeling allow to confirm the proposed mechanisms explaining the unexpected behavior of this glutamate conjugate.

Indexed as

Glutamic AcidSpectrometry, Mass, Electrospray IonizationAmino AcidsAnionsFatty AcidsHumansRegenerationAmino AcidsAnionsFatty AcidsGlutamic AcidIon–dipoleLipidomicLipoamino acidTandem mass spectrometry

Identifiers

PMID35076780
PMCPMC8894203
OpenAlexW4207082725

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.