Evidence map›Paper›PMID 23676762›Full record

ArticleScientific reports2013

Physiologically-relevant modes of membrane interactions by the human antimicrobial peptide, LL-37, revealed by SFG experiments.

Bei Ding, Lauren Soblosky, Khoi Nguyen, Junqing Geng, Xinglong Yu, Ayyalusamy Ramamoorthy, Zhan Chen

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

26 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Review
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  7. Key contributions of a glycolipid to membrane protein integration.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2024
    Review
  8. Article
  9. cGAMP the travelling messenger.Frontiers in immunology · 2023
    Review
  10. Review
  11. Review
  12. Antimicrobial Peptides: A New Hope in Biomedical and Pharmaceutical Fields.Frontiers in cellular and infection microbiology · 2021
    Review
  13. Article
  14. Article
  15. Article
  16. Article
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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

7 authors at 2 institutions in 2 countries.

Bei DingDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.
Lauren Soblosky
Khoi Nguyen
Junqing Geng
Xinglong Yu
Ayyalusamy Ramamoorthy
Zhan Chen
University of Michigan–Ann Arbor · USTsinghua University · CN

Funding

SFG Investigation of Peptide and Protein Orientations in MembranesR01GM081655 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI CHEN, ZHAN · 2008 to 2012
$1.5M
NIGMS NIH HHS R01 GM081655NIGMS NIH HHS R01GM081655
6 · The paper itself

Abstract

Antimicrobial peptides (AMPs) could become the next generation antibiotic compounds which can overcome bacterial resistance by disrupting cell membranes and it is essential to determine the factors underlying its mechanism of action. Although high-resolution NMR and other biological studies have provided valuable insights, it has been a major challenge to follow the AMP-membrane interactions at physiologically-relevant low peptide concentrations. In this study, we demonstrate a novel approach to overcome this major limitation by performing Sum Frequency Generation (SFG) vibrational spectroscopic experiments on lipid bilayers containing an AMP, LL-37. Our results demonstrate the power of SFG to study non-linear helical peptides and also infer that lipid-peptide interaction and the peptide orientation depend on the lipid membrane composition. The observed SFG signal changes capture the aggregating process of LL-37 on membrane. In addition, our SFG results on cholesterol-containing lipid bilayers indicate the inhibition effect of cholesterol on peptide-induced membrane permeation process.

Indexed as

Antimicrobial Cationic PeptidesCathelicidinsHumansLipid BilayersNuclear Magnetic Resonance, BiomolecularAntimicrobial Cationic PeptidesCathelicidinsLipid Bilayers

Identifiers

PMID23676762
PMCPMC3655398
OpenAlexW2114796839

What OpenQuestion holds

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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.