Evidence map›Paper›PMID 22845179›Full record

ArticleThe journal of physical chemistry. B2012

Spectroscopic and computational study of melittin, cecropin A, and the hybrid peptide CM15.

Diana E Schlamadinger, Yi Wang, J Andrew McCammon, Judy E Kim

Open access · bronzeAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.8field-weighted citation impact, top 18% 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

14 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Hydrophobic residues of melittin mediate its binding to αA-crystallin.Protein science : a publication of the Protein Society · 2020
    Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. Article
  13. Single-cell, real-time detection of oxidative stress induced in Escherichia coli by the antimicrobial peptide CM15.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  14. 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

4 authors at 1 institution in 1 country.

Diana E SchlamadingerDepartment of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, California 92093, United States.
Yi Wang
J Andrew McCammon
Judy E Kim
University of California, San Diego · US

Funding

MOLECULAR BIOPHYSICS TRAINING PROGRAMT32GM008326 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KOMIVES, ELIZABETH A. · 1989 to 2020
$7.5M
Howard Hughes Medical InstituteNIGMS NIH HHS GM 08326NIGMS NIH HHS T32 GM008326
6 · The paper itself

Abstract

Antimicrobial peptides (AMPs), such as cecropin A from silk moth, are key components of the innate immune system. They are effective defensive weapons against invading pathogens, yet they do not target host eukaryotic cells. In contrast, peptide toxins, such as honeybee melittin, are nondiscriminating and target both eukaryotic and prokaryotic cells. An AMP-toxin hybrid peptide that is composed of cecropin A and melittin (CM15) improves upon the antimicrobial activity of cecropin A without displaying the nonspecific, hemolytic properties of melittin. Here we report fluorescence and UV resonance Raman spectra of melittin, cecropin A, and CM15 with the goal of elucidating peptide-membrane interactions that help guide specificity. We have probed the potency for membrane disruption, local environment and structure of the single tryptophan residue, backbone conformation near the peptide hinge, and amide backbone structure of the peptides in lipid environments that mimic eukaryotic and prokaryotic membranes. These experimental results suggest that melittin inserts deeply into the bilayer, whereas cecropin A remains localized to the lipid headgroup region. A surprising finding is that CM15 is a potent membrane-disruptor despite its largely unfolded conformation. A molecular dynamics analysis complements these data and demonstrates the ability of CM15 to associate favorably with membranes as an unfolded peptide. This combined experimental-computational study suggests that new models for peptide-membrane interactions should be considered.

Indexed as

Amino Acid SequenceAntimicrobial Cationic PeptidesLipid BilayersMelittenMolecular Dynamics SimulationProtein Structure, SecondarySpectrometry, FluorescenceSpectrum Analysis, RamanAntimicrobial Cationic Peptidesantimicrobial hybrid peptide CM15cecropin ALipid BilayersMelitten

Identifiers

PMID22845179
PMCPMC3434763
OpenAlexW2006684233

What OpenQuestion holds

Textmetadata
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.