Literature DB >> 35841476

Anti-Candida Potential of Peptides from Immature and Ripe Fruits of Capsicum chinense Jacq.

Marilucia C Ribeiro1, Rodrigo S Gebara1, Gabriel B Taveira1, André de O Carvalho1, Rosana Rodrigues2, Erica O Mello1, Celso S Nagano3, Renata P Chaves3, Valdirene M Gomes4.   

Abstract

The objective of this work was to purify and evaluate the antifungal potential of peptides present in immature and ripe fruits of Capsicum chinense Jacq. (accession UENF 1706) on the medical importance yeasts. Initially the proteins of these seedless fruits were extracted, precipitated with ammonium sulfate at 70% saturation, followed by heating at 80 °C. Subsequently, the peptide-rich extract was fractionated by DEAE-Sepharose anion exchange. The whole process was monitored by tricine-SDS-PAGE. The results revealed that the fraction retained in anion exchange column, called D2, of immature and ripe fruits significantly inhibit the growth of Candida albicans and C. tropicalis yeasts. Due to the higher yield, the D2 fraction of immature fruits was selected for further purification by reverse phase chromatography on HPLC, where sixteen different fractions (H1-H16) were obtained and these were subjected to antifungal assay at 50 µg mL-1. Although almost all fractions tested had significant growth inhibition, the HI9 fraction inhibit 99% of the two yeasts tested. The effect of treatment with HI3, HI8, HI9, and HI14 fractions on the viability of yeast cells was analyzed due to their strong growth inhibition. We observed that only 50 μg mL-1 of the HI9 fraction is the lethal dose for 100% of the cells of C. albicans and C. tropicalis in the original assay. Although the HI9 fraction had a fungicidal effect on both tested yeasts, we only observed membrane permeabilization for C. tropicalis cells treated with 50 µg mL-1 of this fraction. Through mass spectrometry, we identified that the 6 kDa peptide band of HI9 fraction showed similarity with antimicrobial peptides belonging to the plant defensin family.
© 2022. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.

Entities:  

Keywords:  Antifungal; Defensin; Mechanism of action; Plant antimicrobial peptide

Year:  2022        PMID: 35841476     DOI: 10.1007/s12602-022-09968-8

Source DB:  PubMed          Journal:  Probiotics Antimicrob Proteins        ISSN: 1867-1306            Impact factor:   5.265


  23 in total

Review 1.  Overview on plant antimicrobial peptides.

Authors:  Ana Maria Benko-Iseppon; Suely Lins Galdino; Tercilio Calsa; Ederson Akio Kido; Alessandro Tossi; Luis Carlos Belarmino; Sergio Crovella
Journal:  Curr Protein Pept Sci       Date:  2010-05       Impact factor: 3.272

Review 2.  Structural aspects of plant antimicrobial peptides.

Authors:  Lara Padovan; Marco Scocchi; Alessandro Tossi
Journal:  Curr Protein Pept Sci       Date:  2010-05       Impact factor: 3.272

3.  Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa.

Authors:  H Schägger; G von Jagow
Journal:  Anal Biochem       Date:  1987-11-01       Impact factor: 3.365

4.  Unravelling the mechanism of action of "de novo" designed peptide P1 with model membranes and gram-positive and gram-negative bacteria.

Authors:  Juan Carlos Espeche; Melina Martínez; Patricia Maturana; Andrea Cutró; Liliana Semorile; Paulo C Maffia; Axel Hollmann
Journal:  Arch Biochem Biophys       Date:  2020-08-21       Impact factor: 4.013

Review 5.  A structural perspective of plant antimicrobial peptides.

Authors:  Marcelo Lattarulo Campos; Luciano Morais Lião; Eliane Santana Fernandes Alves; Ludovico Migliolo; Simoni Campos Dias; Octávio Luiz Franco
Journal:  Biochem J       Date:  2018-11-09       Impact factor: 3.857

Review 6.  Antimicrobial peptides (AMPs): a patent review (2015-2020).

Authors:  Giannamaria Annunziato; Gabriele Costantino
Journal:  Expert Opin Ther Pat       Date:  2020-12-07       Impact factor: 6.674

7.  Snakin-2, an antimicrobial peptide from potato whose gene is locally induced by wounding and responds to pathogen infection.

Authors:  Marta Berrocal-Lobo; Ana Segura; Manuel Moreno; Gemma López; Francisco García-Olmedo; Antonio Molina
Journal:  Plant Physiol       Date:  2002-03       Impact factor: 8.340

8.  Measurement of protein using bicinchoninic acid.

Authors:  P K Smith; R I Krohn; G T Hermanson; A K Mallia; F H Gartner; M D Provenzano; E K Fujimoto; N M Goeke; B J Olson; D C Klenk
Journal:  Anal Biochem       Date:  1985-10       Impact factor: 3.365

9.  Thionin-like peptides from Capsicum annuum fruits with high activity against human pathogenic bacteria and yeasts.

Authors:  Gabriel B Taveira; Luciana S Mathias; Olney V da Motta; Olga L T Machado; Rosana Rodrigues; André O Carvalho; André Teixeira-Ferreira; Jonas Perales; Ilka M Vasconcelos; Valdirene M Gomes
Journal:  Biopolymers       Date:  2014-01       Impact factor: 2.505

10.  Improved protein identification efficiency by mass spectrometry using N-terminal chemical derivatization of peptides from Angiostrongylus costaricensis, a nematode with unknown genome.

Authors:  Ileana R León; Ana G C Neves-Ferreira; Richard H Valente; Ester M Mota; Henrique L Lenzi; Jonas Perales
Journal:  J Mass Spectrom       Date:  2007-06       Impact factor: 1.982

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