Evidence map›Paper›PMID 31251560›Full record

ArticleAnalytical chemistry2019

Native Mass Spectrometry of Antimicrobial Peptides in Lipid Nanodiscs Elucidates Complex Assembly.

Lawrence R Walker, Elaine M Marzluff, Julia A Townsend, William C Resager, Michael T Marty

Abstract read
In one paragraph

Article in Analytical chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

  1. Article
  2. Design of Fluorescent Membrane Scaffold Proteins for Nanodiscs.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Interspecies Variation Affects Islet Amyloid Polypeptide Membrane Binding.Journal of the American Society for Mass Spectrometry · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Deconvolving Native and Intact Protein Mass Spectra with UniDec.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  20. 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

5 authors.

Lawrence R WalkerDepartment of Chemistry and Biochemistry , The University of Arizona , Tucson , Arizona 85721 , United States.
Elaine M MarzluffDepartment of Chemistry , Grinnell College , Grinnell , Iowa 50112 , United States.
Julia A TownsendDepartment of Chemistry and Biochemistry , The University of Arizona , Tucson , Arizona 85721 , United States.
William C ResagerDepartment of Chemistry and Biochemistry , The University of Arizona , Tucson , Arizona 85721 , United States.
Michael T MartyDepartment of Chemistry and Biochemistry , The University of Arizona , Tucson , Arizona 85721 , United States.ORCID 0000-0001-8115-1772

Funding

Unravelling Membrane Protein-Lipid Interactions using Nanodiscs and Mass SpectrometryR35GM128624 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI Michael T Marty · 2018 to 2026
$3.6M
NIGMS NIH HHS R35 GM128624
6 · The paper itself

Abstract

Antimicrobial peptides (AMPs) are generally cationic and amphipathic peptides that show potential applications to combat the growing threat of antibiotic resistant infections. AMPs are known to interact with bacterial membranes, but their mechanisms of toxicity and selectivity are poorly understood, in part because it is challenging to characterize AMP oligomeric complexes within lipid bilayers. Here, we used native mass spectrometry to measure the stoichiometry of AMPs inserted into lipoprotein nanodiscs with different lipid components. Titrations of increasing peptide concentration and collisional activation experiments reveal that AMPs can exhibit a range of behaviors from nonspecific incorporation into the nanodisc to formation of specific complexes. This new approach to characterizing formation of AMP complexes within lipid membranes will provide unique insights into AMP mechanisms.

Indexed as

DimyristoylphosphatidylcholineGramicidinLipid BilayersMass SpectrometryMelittenNanostructuresPhosphatidylglycerolsDimyristoylphosphatidylcholinedimyristoylphosphatidylglycerolGramicidinLipid BilayersMelittenPhosphatidylglycerols

Identifiers

PMID31251560
PMCPMC6635019

What OpenQuestion holds

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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.