Evidence map›Paper›PMID 28230084›Full record

ArticleScientific reports2017

Highly potent antimicrobial peptides from N-terminal membrane-binding region of E. coli MreB.

Karabi Saikia, Yalavarthi Durga Sravani, Vibin Ramakrishnan, Nitin Chaudhary

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.2field-weighted citation impact, top 9% 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

20 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Isobavachalcone exhibits antifungal and antibiofilm effects againstFrontiers in cellular and infection microbiology · 2024
    Article
  7. Drug design, development and therapy · 2024
    Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Conformational Changes of Anoplin, W-MreBInternational journal of molecular sciences · 2020
    Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. 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

4 authors at 1 institution in 1 country.

Karabi SaikiaDepartment of Biosciences and Bioengineering Indian Institute of Technology Guwahati, Guwahati - 781 039, India.
Yalavarthi Durga SravaniDepartment of Biosciences and Bioengineering Indian Institute of Technology Guwahati, Guwahati - 781 039, India.
Vibin RamakrishnanDepartment of Biosciences and Bioengineering Indian Institute of Technology Guwahati, Guwahati - 781 039, India.
Nitin ChaudharyDepartment of Biosciences and Bioengineering Indian Institute of Technology Guwahati, Guwahati - 781 039, India.
Indian Institute of Technology Guwahati · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microbial pathogenesis is a serious health concern. The threat escalates as the existing conventional antimicrobials are losing their efficacy against the evolving pathogens. Peptides hold promise to be developed into next-generation antibiotics. Antimicrobial peptides adopt amphipathic structures that could selectively bind to and disrupt the microbial membranes. Interaction of proteins with membranes is central to all living systems and we reasoned that the membrane-binding domains in microbial proteins could be developed into efficient antimicrobials. This is an interesting approach as self-like sequences could elude the microbial strategies of degrading the antimicrobial peptides, one of the mechanisms of showing resistance to antimicrobials. We selected the 9-residue-long membrane-binding region of E. coli MreB protein. The 9-residue peptide (C-terminal amide) and its N-terminal acetylated analog displayed broad-spectrum activity, killing Gram-negative bacteria, Gram-positive bacteria, and fungi. Extension with a tryptophan residue at the N-terminus drastically improved the activity of the peptides with lethal concentrations ≤10 μM against all the organisms tested. The tryptophan-extended peptides caused complete killing of C. albicans as well as gentamicin and methicillin resistant S. aureus at 5 μM concentration. Lipid-binding studies and electron microscopic analyses of the peptide-treated microbes suggest membrane disruption as the mechanism of killing.

Indexed as

Amino Acid SequenceAnti-Infective AgentsAntimicrobial Cationic PeptidesCandida albicansErythrocytesEscherichia coliEscherichia coli ProteinsGram-Negative BacteriaGram-Positive BacteriaHemolysisHumansKineticsMethicillin-Resistant Staphylococcus aureusMicrobial Sensitivity TestsProtein DomainsSodium ChlorideAnti-Infective AgentsAntimicrobial Cationic PeptidesEscherichia coli ProteinsMreB protein, E coliSodium ChlorideTryptophan

Identifiers

PMID28230084
PMCPMC5322399
OpenAlexW2589488014

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.