Evidence map›Paper›PMID 22103476›Full record

ArticleBiochemistry2011

Using infrared spectroscopy of cyanylated cysteine to map the membrane binding structure and orientation of the hybrid antimicrobial peptide CM15.

Katherine N Alfieri, Alice R Vienneau, Casey H Londergan

Abstract readComparative Study
In one paragraph

Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.2field-weighted citation impact, top 15% 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

13 citing papers in PubMed, 28 citations in OpenAlex.

  1. Site-Specific Interrogation of Protein Structure and Stability.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  2. Article
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  4. Article
  5. Article
  6. Site-specific infrared probes of proteins.Annual review of physical chemistry · 2015
    Review
  7. Article
  8. Article
  9. Calculations of the electric fields in liquid solutions.The journal of physical chemistry. B · 2013
    Article
  10. Article
  11. Article
  12. Article
  13. 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

3 authors at 1 institution in 1 country.

Katherine N AlfieriDepartment of Chemistry, Haverford College, Haverford, Pennsylvania 19041-1392, United States.
Alice R Vienneau
Casey H Londergan
Haverford College · US

Funding

Cyanylated cysteine as vibrational probe of binding-induced structural transitionR15GM088749 · NIGMS · HAVERFORD COLLEGE · PI LONDERGAN, CASEY H · 2009 to 2012
$505k
Howard Hughes Medical InstituteNIGMS NIH HHS R15 GM088749NIGMS NIH HHS R15-GM088749
6 · The paper itself

Abstract

The synthetic antimicrobial peptide CM15, a hybrid of N-terminal sequences from cecropin and melittin peptides, has been shown to be extremely potent. Its mechanism of action has been thought to involve pore formation based on prior site-directed spin labeling studies. This study examines four single-site β-thiocyanatoalanine variants of CM15 in which the artificial amino acid side chain acts as a vibrational reporter of its local environment through the frequency and line shape of the unique CN stretching band in the infrared spectrum. Circular dichroism experiments indicate that the placements of the artificial side chain have only small perturbative effects on the membrane-bound secondary structure of the CM15 peptide. All variant peptides were placed in buffer solution, in contact with dodecylphosphatidylcholine micelles, and in contact with vesicles formed from Escherichia coli polar lipid extract. At each site, the CN stretching band reports a different behavior. Time-dependent attenuated total reflectance infrared spectra were also collected for each variant as it was allowed to remodel the E. coli lipid vesicles. The results of these experiments agree with the previously proposed formation of toroidal pores, in which each peptide finds itself in an increasingly homogeneous and curved local environment without apparent peptide-peptide interactions. This work also demonstrates the excellent sensitivity of the SCN stretching vibration to small changes in the peptide-lipid interfacial structure.

Indexed as

AlanineAlgorithmsAnti-Infective AgentsAntimicrobial Cationic PeptidesCircular DichroismCysteineLauric AcidsLipid BilayersLipid MetabolismLipidsMicellesPhosphatidylcholinesProtein Structure, SecondarySolubilitySpectroscopy, Fourier Transform InfraredSurface PropertiesAlanineAnti-Infective AgentsAntimicrobial Cationic Peptidesantimicrobial hybrid peptide CM15CysteineLauric AcidsLipid BilayersLipidsMicellesPhosphatidylcholinesThiocyanates

Identifiers

PMID22103476
PMCPMC3246368
OpenAlexW2040487718

What OpenQuestion holds

Textmetadata
LicenceTDM
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.