Evidence map›Paper›PMID 30813478›Full record

ArticleMolecules (Basel, Switzerland)2019

Engineering of Antimicrobial Surfaces by Using Temporin Analogs to Tune the Biocidal/antiadhesive Effect.

Pierre-Carl Oger, Christophe Piesse, Ali Ladram, Vincent Humblot

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.7field-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

10 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Temporins: Multifunctional Peptides from Frog Skin.International journal of molecular sciences · 2023
    Review
  5. Review
  6. Designed Multifunctional Peptides for Intracellular Targets.Antibiotics (Basel, Switzerland) · 2022
    Review
  7. Review
  8. Article
  9. Article
  10. 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.

Pierre-Carl OgerSorbonne Université, CNRS, Laboratoire de Réactivité de Surface, LRS UMR CNRS 7197, F-75252 Paris, France. pierre-carl.oger@hotmail.com.
Christophe PiesseSorbonne Université, CNRS, Institut de Biologie Paris-Seine, IBPS, F-75252 Paris, France. christophe.piesse@sorbonne-universite.fr.
Ali LadramSorbonne Université, CNRS, Institut de Biologie Paris-Seine, IBPS, F-75252 Paris, France. ali.ladram@sorbonne-universite.fr.
Vincent HumblotSorbonne Université, CNRS, Laboratoire de Réactivité de Surface, LRS UMR CNRS 7197, F-75252 Paris, France. vincent.humblot@upmc.fr.ORCID 0000-0002-6266-3956
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proliferation of resistant bacteria on biomaterials is a major problem leading to nosocomial infections. Due to their broad-spectrum activity and their ability to disrupt bacterial membranes through a rapid membranolytic mechanism, antimicrobial peptides (AMPs) are less susceptible to the development of bacterial resistance and therefore represent good candidates for surface coating strategies to prevent biofilm formation. In this study, we report on the covalent immobilization of temporin-SHa, a small hydrophobic and low cationic antimicrobial peptide exhibiting broad-spectrum activity, and (SHa) analogs on modified gold surfaces. Several analogs derived from SHa with either a carboxamidated ([K³]SHa, d-[K³]SHa) or a carboxylated C-terminus ([K³]SHa-COOH) were used to achieve peptide grafting on gold surfaces modified by a thiolated self-assembled monolayer (SAM). Surface functionalization was characterized by polarization modulation infrared reflection absorption spectroscopy (PM-RAIRS) and X-ray photoemission spectroscopy (XPS). The antibacterial properties of the temporin-functionalized surfaces were tested against the Gram-positive

Indexed as

Anti-Infective AgentsAntimicrobial Cationic PeptidesBacterial AdhesionBiofilmsDrug Resistance, MicrobialGoldHydrophobic and Hydrophilic InteractionsListeriaProteinsSulfhydryl CompoundsSurface PropertiesAnti-Infective AgentsAntimicrobial Cationic PeptidesGoldProteinsSulfhydryl Compoundstemporinantibacterial/antiadhesive activityantimicrobial peptidesgold surface functionalizationSHa analogstemporin-SHa

Identifiers

PMID30813478
PMCPMC6412374
OpenAlexW2916867230

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.