1. Structural and Biochemical Characterization of Three Antimicrobial Peptides from Capsicum annuum L. var. annuum Leaves for Anti-Candida Use.
- Author
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Cherene MB, Taveira GB, Almeida-Silva F, da Silva MS, Cavaco MC, da Silva-Ferreira AT, Perales JEA, de Oliveira Carvalho A, Venâncio TM, da Motta OV, Rodrigues R, Castanho MARB, and Gomes VM
- Subjects
- Antimicrobial Peptides chemistry, Antimicrobial Peptides pharmacology, Microbial Sensitivity Tests, Plant Proteins pharmacology, Plant Proteins chemistry, Hemolysis drug effects, Plant Extracts pharmacology, Plant Extracts chemistry, Capsicum chemistry, Candida drug effects, Plant Leaves chemistry, Antifungal Agents pharmacology, Antifungal Agents chemistry, Antifungal Agents isolation & purification
- 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., (© 2023. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.)
- Published
- 2024
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