Evidence map›Paper›PMID 31386688›Full record

ArticlePloS one2019

Intragenic antimicrobial peptides (IAPs) from human proteins with potent antimicrobial and anti-inflammatory activity.

Guilherme D Brand, Marcelo H S Ramada, Júlia R Manickchand, Rafael Correa, Dalila J S Ribeiro, Michele A Santos, Andreanne G Vasconcelos, Fernando Y Abrão, Maura V Prates, André M Murad and 5 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

12 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Identification of Novel TAT-I24-Related Peptides with Antiviral Activities.International journal of molecular sciences · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Phylloseptin-1 is Leishmanicidal for Amastigotes ofInternational journal of environmental research and public health · 2020
    Article
  12. 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

15 authors at 3 institutions in 1 country.

Guilherme D BrandLaboratório de Síntese e Análise de Biomoléculas, LSAB, Instituto de Química, Universidade de Brasília, Brasília, DF, Brasil.ORCID 0000-0002-1615-0009
Marcelo H S RamadaPrograma de Pós-Graduação em Ciências Genômicas e Biotecnologia, Universidade Católica de Brasília, Brasília, DF, Brasil.
Júlia R ManickchandLaboratório de Síntese e Análise de Biomoléculas, LSAB, Instituto de Química, Universidade de Brasília, Brasília, DF, Brasil.
Rafael CorreaLaboratório de Imunologia e Inflamação, LIMI, Instituto de Biologia, Universidade de Brasília, Brasília, DF, Brasil.
Dalila J S RibeiroLaboratório de Imunologia e Inflamação, LIMI, Instituto de Biologia, Universidade de Brasília, Brasília, DF, Brasil.
Michele A SantosLaboratório de Ressonância Magnética Nuclear, LRMN, Instituto de Química, Universidade de Brasília, Brasília, DF, Brasil.
Andreanne G VasconcelosNúcleo de Pesquisa em Morfologia e Imunologia Aplicada, NuPMIA, Faculdade de Medicina, Campus Universitário Darcy Ribeiro, Universidade de Brasília, Brasília, DF, Brasil.
Fernando Y AbrãoFaculdade de Farmácia, FacUnicamps, Goiânia, GO, Brasil.
Maura V PratesLaboratório de Espectrometria de Massa, LEM, Embrapa Recursos Genéticos e Biotecnologia, Brasília, DF, Brasil.
André M MuradLaboratório de Espectrometria de Massa, LEM, Embrapa Recursos Genéticos e Biotecnologia, Brasília, DF, Brasil.
José L Cardozo FhLaboratório de Espectrometria de Massa, LEM, Embrapa Recursos Genéticos e Biotecnologia, Brasília, DF, Brasil.
José Roberto S A LeiteNúcleo de Pesquisa em Morfologia e Imunologia Aplicada, NuPMIA, Faculdade de Medicina, Campus Universitário Darcy Ribeiro, Universidade de Brasília, Brasília, DF, Brasil.
Kelly G MagalhãesLaboratório de Imunologia e Inflamação, LIMI, Instituto de Biologia, Universidade de Brasília, Brasília, DF, Brasil.
Aline L OliveiraLaboratório de Ressonância Magnética Nuclear, LRMN, Instituto de Química, Universidade de Brasília, Brasília, DF, Brasil.ORCID 0000-0002-6928-078X
Carlos BlochLaboratório de Espectrometria de Massa, LEM, Embrapa Recursos Genéticos e Biotecnologia, Brasília, DF, Brasil.
Universidade de Brasília · BRBrazilian Agricultural Research Corporation · BRFundação de Apoio a Pesquisa do Estado de Goiás · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Following the treads of our previous works on the unveiling of bioactive peptides encrypted in plant proteins from diverse species, the present manuscript reports the occurrence of four proof-of-concept intragenic antimicrobial peptides in human proteins, named Hs IAPs. These IAPs were prospected using the software Kamal, synthesized by solid phase chemistry, and had their interactions with model phospholipid vesicles investigated by differential scanning calorimetry and circular dichroism. Their antimicrobial activity against bacteria, yeasts and filamentous fungi was determined, along with their cytotoxicity towards erythrocytes. Our data demonstrates that Hs IAPs are capable to bind model membranes while attaining α-helical structure, and to inhibit the growth of microorganisms at concentrations as low as 1μM. Hs02, a novel sixteen residue long internal peptide (KWAVRIIRKFIKGFIS-NH2) derived from the unconventional myosin 1h protein, was further investigated in its capacity to inhibit lipopolysaccharide-induced release of TNF-α in murine macrophages. Hs02 presented potent anti-inflammatory activity, inhibiting the release of TNF-α in LPS-primed cells at the lowest assayed concentration, 0.1 μM. A three-dimensional solution structure of Hs02 bound to DPC micelles was determined by Nuclear Magnetic Resonance. Our work exemplifies how the human genome can be mined for molecules with biotechnological potential in human health and demonstrates that IAPs are actual alternatives to antimicrobial peptides as pharmaceutical agents or in their many other putative applications.

Indexed as

AnimalsAnti-Infective AgentsAnti-Inflammatory AgentsErythrocytesHumansLiposomesMacrophagesMiceMicellesPeptidesProtein Conformation, alpha-HelicalProteinsSolid-Phase Synthesis TechniquesTumor Necrosis Factor-alphaAnti-Infective AgentsAnti-Inflammatory AgentsLiposomesMicellesPeptidesProteinsTumor Necrosis Factor-alpha

Identifiers

PMID31386688
PMCPMC6684085
OpenAlexW2966006321

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.