Evidence map›Paper›PMID 34406694›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2021

A Diazirine-Modified Membrane Lipid to Study Peptide/Lipid Interactions - Chances and Challenges.

Julia Dorner, Patricia Korn, Kai Gruhle, Daniel Ramsbeck, Vasil M Garamus, Hauke Lilie, Annette Meister, Christian Schwieger, Christian Ihling, Andrea Sinz and 1 more

Abstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Bioconjugation Strategies for Revealing the Roles of Glycerophospholipids in Cells.Chembiochem : a European journal of chemical biology · 2026
    Review
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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

11 authors.

Julia DornerInstitute of Pharmacy-Pharmaceutical Chemistry and Bioanalytics, Martin Luther University (MLU) Halle-Wittenberg, Kurt-Mothes-Str. 3, 06120, Halle (Saale), Germany.
Patricia KornInstitute of Pharmacy-Pharmaceutical Chemistry and Bioanalytics, Martin Luther University (MLU) Halle-Wittenberg, Kurt-Mothes-Str. 3, 06120, Halle (Saale), Germany.
Kai GruhleInstitute of Pharmacy-Pharmaceutical Chemistry and Bioanalytics, Martin Luther University (MLU) Halle-Wittenberg, Kurt-Mothes-Str. 3, 06120, Halle (Saale), Germany.
Daniel RamsbeckFraunhofer Institute for Cell Therapy and Immunology IZI, Weinbergweg 22, 06120, Halle (Saale), Germany.ORCID http://orcid.org/0000-0002-4966-142X
Vasil M GaramusHelmholtz-Zentrum Hereon, Max-Planck-Str. 1, 21502, Geesthacht, Germany.ORCID http://orcid.org/0000-0001-9315-4188
Hauke LilieInstitute for Biochemistry and Biotechnology-Technical Biochemistry, MLU Halle-Wittenberg, Kurt-Mothes-Str. 3, 06120, Halle (Saale), Germany.
Annette MeisterInstitute of Biochemistry and Biotechnology-Physical Biotechnology Charles Tanford Protein Center, MLU Halle-Wittenberg, Kurt-Mothes-Str. 3a, 06120, Halle (Saale), Germany.ORCID http://orcid.org/0000-0003-1668-4382
Christian SchwiegerInterdisciplinary Research Center HALOmem, MLU Halle-Wittenberg Charles Tanford Protein Center, Kurt-Mothes-Str. 3a, 06120, Halle (Saale), Germany.ORCID http://orcid.org/0000-0001-8327-1233
Christian IhlingInstitute of Pharmacy-Pharmaceutical Chemistry and Bioanalytics, Martin Luther University (MLU) Halle-Wittenberg, Kurt-Mothes-Str. 3, 06120, Halle (Saale), Germany.
Andrea SinzInstitute of Pharmacy-Pharmaceutical Chemistry and Bioanalytics, Martin Luther University (MLU) Halle-Wittenberg, Kurt-Mothes-Str. 3, 06120, Halle (Saale), Germany.ORCID http://orcid.org/0000-0003-1521-4899
Simon DrescherInstitute of Pharmacy-Biophysical Pharmacy, MLU Halle-Wittenberg, Wolfgang-Langenbeck-Str. 4, 06120, Halle (Saale), Germany.ORCID http://orcid.org/0000-0002-3272-1721

Funding

Deutsche Forschungsgemeinschaft Si 867/15-2
6 · The paper itself

Abstract

Although incorporation of photo-activatable lipids into membranes potentially opens up novel avenues for investigating interactions with proteins, the question of whether diazirine-modified lipids are suitable for such studies, remains under debate. Focusing on the potential for studying lipid/peptide interactions by cross-linking mass spectrometry (XL-MS), we developed a diazirine-modified lipid (DiazPC), and examined its behaviour in membranes incorporating the model α-helical peptide LAVA20. We observed an unexpected backfolding of the diazirine-containing stearoyl chain of the lipid. This surprising behaviour challenges the potential application of DiazPC for future XL-MS studies of peptide and protein/lipid interactions. The observations made for DiazPC most likely represent a general phenomenon for any type of membrane lipids with a polar moiety incorporated into the alkyl chain. Our finding is therefore of importance for future protein/lipid interaction studies relying on modified lipid probes.

Indexed as

DiazomethaneMembrane LipidsCross-Linking ReagentsMass SpectrometryPeptidesCross-Linking ReagentsDiazomethaneMembrane LipidsPeptidesdiazirinemass spectrometrymembrane lipidsmiscibilitypeptide/lipid interactionsphoto-cross-linkingXL-MS

Identifiers

PMID34406694
PMCPMC8597076

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.