Evidence map›Paper›PMID 42886166›Full record

ArticleThe Analyst2026

Probing non-covalent membrane protein-lipid interactions using sheath liquid capillary electrophoresis-native top-down mass spectrometry.

Kanchan Pathak, Delaynie Brinkman, Sara Walters, Gustavo Perrotti, Brian Fuglestad, Fabio P Gomes

Abstract read
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Article in The Analyst, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Kanchan PathakDepartment of Chemistry, Virginia Commonwealth University, Richmond, Virginia 23284, USA. pereiragomf@vcu.edu.
Delaynie BrinkmanDepartment of Chemistry, Virginia Commonwealth University, Richmond, Virginia 23284, USA. pereiragomf@vcu.edu.
Sara WaltersDepartment of Chemistry, Virginia Commonwealth University, Richmond, Virginia 23284, USA. pereiragomf@vcu.edu.
Gustavo PerrottiDepartment of Chemistry, Virginia Commonwealth University, Richmond, Virginia 23284, USA. pereiragomf@vcu.edu.
Brian FuglestadDepartment of Chemistry, Virginia Commonwealth University, Richmond, Virginia 23284, USA. pereiragomf@vcu.edu.ORCID http://orcid.org/0000-0001-8304-8269
Fabio P GomesDepartment of Chemistry, Virginia Commonwealth University, Richmond, Virginia 23284, USA. pereiragomf@vcu.edu.ORCID http://orcid.org/0000-0003-0542-6820

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Probing non-covalent membrane protein-lipid interactions remains challenging due to the high hydrophobicity and aggregation propensity of membrane proteins. Here, we present a sheath liquid capillary electrophoresis-native top-down mass spectrometry (CE-nTDMS) platform that enables reproducible infusion of aquaporin Z-cardiolipin assemblies and preserves their non-covalent electrostatic interactions during top-down fragmentation. This workflow generated a diagnostic fragment ion that localizes a lipid-binding region within the protein backbone. Notably, charge-reduced precursor fragment ions of the lipid-bound assembly exhibited asymmetrical isotopic distributions following collisional activation, while corresponding apo precursors displayed symmetrical isotopic distributions. These findings demonstrate the utility of CE-nTDMS for reliable analysis of membrane protein-lipid assemblies and provide new insight into the behavior of lipid-bound fragments during collisional activation.

Identifiers

PMID42886166

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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.