Evidence map›Paper›PMID 33454869›Full record

ArticleProbiotics and antimicrobial proteins2021

Potent Anti-Candida Fraction Isolated from Capsicum chinense Fruits Contains an Antimicrobial Peptide That is Similar to Plant Defensin and is Able to Inhibit the Activity of Different α-Amylase Enzymes.

Mariana C L Aguieiras, Larissa M Resende, Thaynã A M Souza, Celso S Nagano, Renata P Chaves, Gabriel B Taveira, André O Carvalho, Rosana Rodrigues, Valdirene M Gomes, Érica O Mello

Abstract read
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In one paragraph

Article in Probiotics and antimicrobial proteins, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

14 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Cliotide U1, a Novel Antimicrobial Peptide Isolated FromBioinformatics and biology insights · 2025
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Non-Journal of fungi (Basel, Switzerland) · 2022
    Review
  12. Journal of food science and technology · 2022
    Review
  13. Immunomodulatory and Allergenic Properties of Antimicrobial Peptides.International journal of molecular sciences · 2022
    Review
  14. Review
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

10 authors at 2 institutions in 1 country.

Mariana C L AguieirasLaboratório de Fisiologia E Bioquímica de Microrganismos, Centro de Biociências E Biotecnologia, Universidade Estadual Do Norte Fluminense Darcy Ribeiro, Avenida Alberto Lamego, 2000, Campos dos Goytacazes, RJ, Brazil.
Larissa M ResendeLaboratório de Fisiologia E Bioquímica de Microrganismos, Centro de Biociências E Biotecnologia, Universidade Estadual Do Norte Fluminense Darcy Ribeiro, Avenida Alberto Lamego, 2000, Campos dos Goytacazes, RJ, Brazil.
Thaynã A M SouzaLaboratório de Fisiologia E Bioquímica de Microrganismos, Centro de Biociências E Biotecnologia, Universidade Estadual Do Norte Fluminense Darcy Ribeiro, Avenida Alberto Lamego, 2000, Campos dos Goytacazes, RJ, Brazil.
Celso S NaganoLaboratório de Bioquímica Marinha, Departamento de Engenharia de Pesca, Universidade Federal Do Ceará, Fortaleza, CE, Brazil.
Renata P ChavesLaboratório de Bioquímica Marinha, Departamento de Engenharia de Pesca, Universidade Federal Do Ceará, Fortaleza, CE, Brazil.
Gabriel B TaveiraLaboratório de Fisiologia E Bioquímica de Microrganismos, Centro de Biociências E Biotecnologia, Universidade Estadual Do Norte Fluminense Darcy Ribeiro, Avenida Alberto Lamego, 2000, Campos dos Goytacazes, RJ, Brazil.
André O CarvalhoLaboratório de Fisiologia E Bioquímica de Microrganismos, Centro de Biociências E Biotecnologia, Universidade Estadual Do Norte Fluminense Darcy Ribeiro, Avenida Alberto Lamego, 2000, Campos dos Goytacazes, RJ, Brazil.
Rosana RodriguesLaboratório de Melhoramento E Genética Vegetal, Centro de Ciências E Tecnologias Agropecuárias, Universidade Estadual Do Norte Fluminense Darcy Ribeiro, Campos dos Goytacazes, RJ, Brazil.
Valdirene M GomesLaboratório de Fisiologia E Bioquímica de Microrganismos, Centro de Biociências E Biotecnologia, Universidade Estadual Do Norte Fluminense Darcy Ribeiro, Avenida Alberto Lamego, 2000, Campos dos Goytacazes, RJ, Brazil. valmguenf@gmail.com.
Érica O MelloLaboratório de Fisiologia E Bioquímica de Microrganismos, Centro de Biociências E Biotecnologia, Universidade Estadual Do Norte Fluminense Darcy Ribeiro, Avenida Alberto Lamego, 2000, Campos dos Goytacazes, RJ, Brazil. ericamello08@gmail.com.ORCID 0000-0002-1965-4560
State University of Norte Fluminense · BRUniversidade Federal do Ceará · BR

Funding

Lacrimal Gland Repair Using Progenitor CellsR01EY026202 · NEI · SCRIPPS RESEARCH INSTITUTE, THE · PI MAKARENKOVA, HELEN P. · 2016 to 2025
$5.2M
6 · The paper itself

Abstract

Antimicrobial peptides (AMPs) are molecules present in several life forms, possess broad-spectrum of inhibitory activity against pathogenic microorganisms, and are a promising alternative to combat the multidrug resistant pathogens. The aim of this work was to identify and characterize AMPs from Capsicum chinense fruits and to evaluate their inhibitory activities against yeasts of the genus Candida and α-amylases. Initially, after protein extraction from fruits, the extract was submitted to anion exchange chromatography resulting two fractions. Fraction D1 was further fractionated by molecular exclusion chromatography, and three fractions were obtained. These fractions showed low molecular mass peptides, and in fraction F3, only two protein bands of approximately 6.5 kDa were observed. Through mass spectrometry, we identified that the lowest molecular mass protein band of fraction F3 showed similarity with AMPs from plant defensin family. We named this peptide CcDef3 (Capsicum chinense defensin 3). The antifungal activity of these fractions was analyzed against yeasts of the genus Candida. At 200 μg/mL, fraction F1 inhibited the growth of C. tropicalis by 26%, fraction F2 inhibited 35% of the growth of C. buinensis, and fraction F3 inhibited all tested yeasts, exhibiting greater inhibition activity on the growth of the yeast C. albicans (86%) followed by C. buinensis (69%) and C. tropicalis (21%). Fractions F1 and F2 promoted membrane permeabilization of all tested yeasts and increased the endogenous induction of reactive oxygen species (ROS) in C. buinensis and C. tropicalis, respectively. We also observed that fraction F3 at a concentration of 50 µg/mL inhibited the α-amylase activities of Tenebrio molitor larvae by 96% and human salivary by 100%. Thus, our results show that fraction F3, which contains CcDef3, is a very promising protein fraction because it has antifungal potential and is able to inhibit the activity of different α-amylase enzymes.

Indexed as

Antifungal AgentsCapsicumalpha-AmylasesAntimicrobial PeptidesCandidaDefensinsFruitHumansPhytochemicalsalpha-AmylasesAntifungal AgentsAntimicrobial PeptidesDefensinsPhytochemicalsAntifungalMechanism of actionPlant antimicrobial peptideα-Amylase

Identifiers

PMID33454869
OpenAlexW3122152141

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.