Evidence map›Paper›PMID 25109311›Full record

ArticleScientific reports2014

Controlling resistant bacteria with a novel class of β-lactamase inhibitor peptides: from rational design to in vivo analyses.

Santi M Mandal, Ludovico Migliolo, Osmar N Silva, Isabel C M Fensterseifer, Celio Faria-Junior, Simoni C Dias, Amit Basak, Tapas K Hazra, Octávio L Franco

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.8field-weighted citation impact, top 34% 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

11 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Synthetic antibiofilm peptides.Biochimica et biophysica acta · 2016
    Review
  11. 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 4 institutions in 3 countries.

Santi M Mandal1] Central Research Facility, Department of Chemistry, Indian Institute of Technology Kharagpur, Kharagpur 721302, WB, India [2].
Ludovico Migliolo1] Programa de Pós-Graduação em Ciências Genômicas e Biotecnologia, Centro de Análises, Proteômicas e Bioquímicas, Universidade Católica de Brasília, Brazil [2] Pos-Graducao em Biotecnologia, Universidade Católica Dom Bosco, Campo Grande, MS, Brazil [3].
Osmar N Silva1] Programa de Pós-Graduação em Ciências Genômicas e Biotecnologia, Centro de Análises, Proteômicas e Bioquímicas, Universidade Católica de Brasília, Brazil [2].
Isabel C M FensterseiferPrograma de Pós-Graduação em Ciências Genômicas e Biotecnologia, Centro de Análises, Proteômicas e Bioquímicas, Universidade Católica de Brasília, Brazil.
Celio Faria-JuniorLacen, Laboratório Central de Saúde Publica do Distrito Federal, Brasília, DF, Brazil.
Simoni C DiasPrograma de Pós-Graduação em Ciências Genômicas e Biotecnologia, Centro de Análises, Proteômicas e Bioquímicas, Universidade Católica de Brasília, Brazil.
Amit BasakCentral Research Facility, Department of Chemistry, Indian Institute of Technology Kharagpur, Kharagpur 721302, WB, India.
Tapas K HazraDepartment of Internal Medicine, University of Texas Medical Branch, Galveston; TX 77555, USA.
Octávio L Franco1] Programa de Pós-Graduação em Ciências Genômicas e Biotecnologia, Centro de Análises, Proteômicas e Bioquímicas, Universidade Católica de Brasília, Brazil [2] Pos-Graducao em Biotecnologia, Universidade Católica Dom Bosco, Campo Grande, MS, Brazil.
Universidade Católica de Brasília · BRIndian Institute of Technology Kharagpur · INThe University of Texas Medical Branch at Galveston · USUniversidade Católica Dom Bosco · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peptide rational design was used here to guide the creation of two novel short β-lactamase inhibitors, here named dBLIP-1 and -2, with length of five amino acid residues. Molecular modeling associated with peptide synthesis improved bactericidal efficacy in addition to amoxicillin, ampicillin and cefotaxime. Docked structures were consistent with calorimetric analyses against bacterial β-lactamases. These two compounds were further tested in mice. Whereas commercial antibiotics alone failed to cure mice infected with Staphylococcus aureus and Escherichia coli expressing β-lactamases, infection was cleared when treated with antibiotics in combination with dBLIPs, clearly suggesting that peptides were able to neutralize bacterial resistance. Moreover, immunological assays were also performed showing that dBLIPs were unable to modify mammalian immune response in both models, reducing the risks of collateral effects. In summary, the unusual peptides here described provide leads to overcome β-lactamase-based resistance, a remarkable clinical challenge.

Indexed as

Drug DesignAnimalsAnti-Bacterial AgentsBacillus cereusbeta-Lactamase Inhibitorsbeta-LactamasesBinding SitesCell LineCell SurvivalDrug Resistance, BacterialErythrocytesEscherichia coliKineticsMiceMicrobial Sensitivity TestsMolecular Docking SimulationAnti-Bacterial Agentsbeta-Lactamase Inhibitorsbeta-LactamasesPeptides

Identifiers

PMID25109311
PMCPMC4127500
OpenAlexW2035548245

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.