Evidence map›Paper›PMID 27292548›Full record

ArticleScientific reports2016

Structural Studies of a Lipid-Binding Peptide from Tunicate Hemocytes with Anti-Biofilm Activity.

Osmar N Silva, Eliane S F Alves, César de la Fuente-Núñez, Suzana M Ribeiro, Santi M Mandal, Diana Gaspar, Ana S Veiga, Miguel A R B Castanho, Cesar A S Andrade, Jessica M Nascimento and 8 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed, 1 pooled it
4.3field-weighted citation impact, top 6% 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

13 citing papers in PubMed, 1 synthesis or guideline pooled it, 29 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Antibiofilm peptides against oral biofilms.Journal of oral microbiology · 2017
    Article
  13. 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

18 authors at 8 institutions in 4 countries.

Osmar N SilvaDepartamento Biologia, Instituto de Ciências Biológicas, Programa de pós-graduação em Genética e Biotecnologia, Universidade Federal de Juiz de Fora, Juiz de Fora-MG, 36036-900, Brazil.
Eliane S F AlvesLaboratório de RMN, Instituto de Química, Universidade Federal de Goiás, C.P. 131, 74001-970 Goiânia, GO, Brazil.
César de la Fuente-NúñezDepartment of Microbiology and Immunology, University of British Columbia, Vancouver, British Columbia, Canada.
Suzana M RibeiroSInova, Pós-graduação em Biotecnologia, Universidade Católica Dom Bosco, Campo Grande, MS, Brazil.
Santi M MandalCentral Research Facility, Department of Chemistry and Department of Biotechnology, Indian Institute of Technology Kharagpur, India.
Diana GasparInstituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Av. Prof. Egas Moniz, 1649-028 Lisbon, Portugal.
Ana S VeigaInstituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Av. Prof. Egas Moniz, 1649-028 Lisbon, Portugal.
Miguel A R B CastanhoInstituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Av. Prof. Egas Moniz, 1649-028 Lisbon, Portugal.
Cesar A S AndradePrograma de Pós-Graduação em Inovação Terapêutica, Universidade Federal de Pernambuco, 50670-901 Recife, PE, Brazil.
Jessica M NascimentoPrograma de Pós-Graduação em Inovação Terapêutica, Universidade Federal de Pernambuco, 50670-901 Recife, PE, Brazil.
Isabel C M FensterseiferSInova, Pós-graduação em Biotecnologia, Universidade Católica Dom Bosco, Campo Grande, MS, Brazil.
William F PortoSInova, Pós-graduação em Biotecnologia, Universidade Católica Dom Bosco, Campo Grande, MS, Brazil.
Jose R CorreaDepartment of Cellular Biology, Institute of Biological Sciences, University of Brasilia, Brasilia, 70910900, Brazil.
Robert E W HancockDepartment of Microbiology and Immunology, University of British Columbia, Vancouver, British Columbia, Canada.
Suresh KorpoleCentral Research Facility, Department of Chemistry and Department of Biotechnology, Indian Institute of Technology Kharagpur, India.
Aline L OliveiraLaboratório de RMN, Instituto de Química, Universidade Federal de Goiás, C.P. 131, 74001-970 Goiânia, GO, Brazil.
Luciano M LiaoLaboratório de RMN, Instituto de Química, Universidade Federal de Goiás, C.P. 131, 74001-970 Goiânia, GO, Brazil.
Octavio L FrancoDepartamento Biologia, Instituto de Ciências Biológicas, Programa de pós-graduação em Genética e Biotecnologia, Universidade Federal de Juiz de Fora, Juiz de Fora-MG, 36036-900, Brazil.
Universidade Católica Dom Bosco · BRUniversity of Lisbon · PTIndian Institute of Technology Kharagpur · INUniversidade de Brasília · BRUniversidade Federal de Goiás · BRUniversidade Federal de Pernambuco · BRUniversity of British Columbia · CAUniversidade Católica de Brasília · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Clavanins is a class of peptides (23aa) histidine-rich, free of post-translational modifications. Clavanins have been studied largely for their ability to disrupt bacterial membranes. In the present study, the interaction of clavanin A with membranes was assessed by dynamic light scattering, zeta potential and permeabilization assays. We observed through those assays that clavanin A lysis bacterial cells at concentrations corresponding to its MIC. Further, the structure and function of clavanin A was investigated. To better understand how clavanin interacted with bacteria, its NMR structure was elucidated. The solution state NMR structure of clavanin A in the presence of TFE-d3 indicated an α-helical conformation. Secondary structures, based on circular dichroism measurements in anionic sodium dodecyl sulfate (SDS) and TFE (2,2,2-trifluorethanol), in silico lipid-peptide docking and molecular simulations with lipids DPPC and DOPC revealed that clavanin A can adopt a variety of folds, possibly influencing its different functions. Microcalorimetry assays revealed that clavanin A was capable of discriminating between different lipids. Finally, clavanin A was found to eradicate bacterial biofilms representing a previously unrecognized function.

Indexed as

AnimalsBacteriaBacterial Physiological PhenomenaBiofilmsBlood ProteinsCell MembraneCircular DichroismDynamic Light ScatteringHemocytesLipid BilayersMicrobial Sensitivity TestsMolecular Docking SimulationProtein Structure, SecondaryUrochordataBlood Proteinsclavanin ALipid Bilayers

Identifiers

PMID27292548
PMCPMC4904370
OpenAlexW2422419779

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.