Evidence map›Paper›PMID 33615169›Full record

ArticleACS pharmacology & translational science2021

Old Polyanionic Drug Suramin Suppresses Detrimental Cytotoxicity of the Host Defense Peptide LL-37.

Mayra Quemé-Peña, Maria Ricci, Tünde Juhász, Kata Horváti, Szilvia Bősze, Beáta Biri-Kovács, Bálint Szeder, Ferenc Zsila, Tamás Beke-Somfai

Open access · greenAbstract read
In one paragraph

Article in ACS pharmacology & translational science, 2021. 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
1.3field-weighted citation impact, top 21% 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, 13 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Quorum SensingFrontiers in molecular biosciences · 2021
    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

9 authors at 3 institutions in 1 country.

Mayra Quemé-PeñaInstitute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Biomolecular Self-Assembly Research Group, Budapest H-1117, Hungary.
Maria RicciInstitute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Biomolecular Self-Assembly Research Group, Budapest H-1117, Hungary.
Tünde JuhászInstitute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Biomolecular Self-Assembly Research Group, Budapest H-1117, Hungary.
Kata HorvátiMTA-ELTE Research Group of Peptide Chemistry, Eötvös Loránd University, Hungarian Academy of Sciences, Budapest H-1117, Hungary.
Szilvia BőszeMTA-ELTE Research Group of Peptide Chemistry, Eötvös Loránd University, Hungarian Academy of Sciences, Budapest H-1117, Hungary.
Beáta Biri-KovácsMTA-ELTE Research Group of Peptide Chemistry, Eötvös Loránd University, Hungarian Academy of Sciences, Budapest H-1117, Hungary.
Bálint SzederInstitute of Enzymology, Research Centre for Natural Sciences, Budapest H-1117, Hungary.
Ferenc ZsilaInstitute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Biomolecular Self-Assembly Research Group, Budapest H-1117, Hungary.
Tamás Beke-SomfaiInstitute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Biomolecular Self-Assembly Research Group, Budapest H-1117, Hungary.
Eötvös Loránd University · HUInstitute of Materials and Environmental Chemistry · HUInstitute of Molecular Life Sciences · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The host defense peptide LL-37 is the only human cathelicidin, characterized by pleiotropic activity ranging from immunological to anti-neoplastic functions. However, its overexpression has been associated with harmful inflammatory responses and apoptosis. Thus, for the latter cases, the development of strategies aiming to reduce LL-37 toxicity is highly desired as these have the potential to provide a viable solution. Here, we demonstrate that the reduction of LL-37 toxicity might be achieved by the impairment of its cell surface binding through interaction with small organic compounds that are able to alter the peptide conformation and minimize its cell penetration ability. In this regard, the performed cell viability and internalization studies showed a remarkable attenuation of LL-37 cytotoxicity toward colon and monocytic cells in the presence of the polysulfonated drug suramin. The mechanistic examinations of the molecular details indicated that this effect was coupled with the ability of suramin to alter LL-37 secondary structure

Identifiers

PMID33615169
PMCPMC7887748
OpenAlexW3109704331

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.