Evidence map›Paper›PMID 28447030›Full record

ReviewFrontiers in chemistry2017

Screening and Optimizing Antimicrobial Peptides by Using SPOT-Synthesis.

Paula M López-Pérez, Elizabeth Grimsey, Luc Bourne, Ralf Mikut, Kai Hilpert

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.6field-weighted citation impact, top 8% 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

25 citing papers in PubMed, 50 citations in OpenAlex.

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  12. Article
  13. Engineering Selectively Targeting Antimicrobial Peptides.Annual review of biomedical engineering · 2021
    Review
  14. Article
  15. Potent intracellular antibacterial activity of a marine peptide-N6NHApplied microbiology and biotechnology · 2021
    Article
  16. Article
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  18. Review
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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

5 authors at 3 institutions in 2 countries.

Paula M López-PérezTiKa Diagnostics LtdLondon, UK.
Elizabeth GrimseyInstitute for Infection and Immunity, St. George's University of LondonLondon, UK.
Luc BourneInstitute for Infection and Immunity, St. George's University of LondonLondon, UK.
Ralf MikutKarlsruhe Institute of Technology (KIT), Institute for Applied Computer Science (IAI)Eggenstein-Leopoldshafen, Germany.
Kai HilpertTiKa Diagnostics LtdLondon, UK.
St George's, University of London · GBKarlsruhe Institute of Technology · DEQuest Diagnostics (United Kingdom) · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peptide arrays on cellulose are a powerful tool to investigate peptide interactions with a number of different molecules, for examples antibodies, receptors or enzymes. Such peptide arrays can also be used to study interactions with whole cells. In this review, we focus on the interaction of small antimicrobial peptides with bacteria. Antimicrobial peptides (AMPs) can kill multidrug-resistant (MDR) human pathogenic bacteria and therefore could be next generation antibiotics targeting MDR bacteria. We describe the screen and the result of different optimization strategies of peptides cleaved from the membrane. In addition, screening of antibacterial activity of peptides that are tethered to the surface is discussed. Surface-active peptides can be used to protect surfaces from bacterial infections, for example implants.

Indexed as

antimicrobial peptidesantimicrobial screeningmulti-drug resistancepeptide librariespeptide synthesisSPOT-synthesissubstitution analysistethered peptides

Identifiers

PMID28447030
PMCPMC5388751
OpenAlexW2607129213

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.