ArticleProbiotics and antimicrobial proteins2024
Structural and Biochemical Characterization of Three Antimicrobial Peptides from Capsicum annuum L. var. annuum Leaves for Anti-Candida Use.
Article in Probiotics and antimicrobial proteins, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Antifungal Potential of Peptide-Enriched Fractions Isolated from Capsicum frutescens Seeds Against Yeasts of the Genus Candida.Probiotics and antimicrobial proteins · 2026Article
- Natural and Synthetic AMPs from Latin America across Diversity Engineering and Applications.ACS infectious diseases · 2026Review
- Article
- Characterization and Antifungal Activity of a Hevein-Like Peptide-Containing Extract FromInternational journal of microbiology · 2026Article
- Article
- Exploring the Chemical Features and Biomedical Relevance of Cell-Penetrating Peptides.International journal of molecular sciences · 2024Review
- Plant Antimicrobial Peptides and Their Main Families and Roles: A Review of the Literature.Current issues in molecular biology · 2024Review
- Antifungal Plant Defensins as an Alternative Tool to Combat Candidiasis.Plants (Basel, Switzerland) · 2024Review
- Carboxypeptidase inhibitors fromFrontiers in molecular biosciences · 2023Article
Corrections and comments
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Authors and funding
13 authors.
Funding
Abstract
The emergence of resistant microorganisms has reduced the effectiveness of currently available antimicrobials, necessitating the development of new strategies. Plant antimicrobial peptides (AMPs) are promising candidates for novel drug development. In this study, we aimed to isolate, characterize, and evaluate the antimicrobial activities of AMPs isolated from Capsicum annuum. The antifungal potential was tested against Candida species. Three AMPs from C. annuum leaves were isolated and characterized: a protease inhibitor, a defensin-like protein, and a lipid transporter protein, respectively named CaCPin-II, CaCDef-like, and CaCLTP2. All three peptides had a molecular mass between 3.5 and 6.5 kDa and caused morphological and physiological changes in four different species of the genus Candida, such as pseudohyphae formation, cell swelling and agglutination, growth inhibition, reduced cell viability, oxidative stress, membrane permeabilization, and metacaspase activation. Except for CaCPin-II, the peptides showed low or no hemolytic activity at the concentrations used in the yeast assays. CaCPin-II inhibited α-amylase activity. Together, these results suggest that these peptides have the potential as antimicrobial agents against species of the genus Candida and can serve as scaffolds for the development of synthetic peptides for this purpose.
Indexed as
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Registered trials
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.