Abstract
Due to the increasing rate of invasive fungal infections and emerging antifungal resistance, development of novel antifungal drugs has been an urgent necessity. Antifungal peptides (AFPs) have recently attracted attention due to their unique ability to evade drug-resistant fungal pathogens. In this study, a novel AFP, Cc-AFP1, with a molecular weight of ~3.759 kDa, was isolated from Carum carvi L., purified by ammonium sulfate precipitation and reversed-phase HPLC and finally identified by sequence analysis using Edman degradation. Peptide sequence analysis revealed a fragment of 36 amino acid residues as RVCFRPVAPYLGVGVSGAVRDQIGVKLGSVYKGPRG for Cc-AFP1 with a net charge of +5 and a hydrophobicity ratio of 38%. The antifungal activity of Cc-AFP1 was confirmed against Aspergillus species with MIC values in the range of 8–16 µg/ml. Cc-AFP1 had less than 5% hemolytic activity at 8–16 µg/ml on human red blood cells with no obvious cytotoxicity against the HEK293 cell line. Stability analysis showed that the activity of Cc-AFP1 was maintained at different temperatures (20°C to 80°C) and pH (8 to 10). The results of a propidium iodide uptake and transmission electron microscopy showed that the antifungal activity of Cc-AFP1 could be attributed to alteration in the fungal cell membrane permeability. Taken together, these results indicate that Cc-AFP1 may be an attractive molecule to develop as a novel antifungal agent combating fungal infections cause by Aspergillus species.
Highlights
In the past two decades, there has been an increase in the prevalence of life-threatening fungal infections leading to high morbidity and mortality (Firacative, 2020)
Antifungal peptides (AFPs) which originated from natural sources such as plants and microorganisms gained increasing attention as therapeutic agents in recent years owing to several advantages, including high selectivity and effectiveness, low immunogenicity, and good penetration to host organs and tissues (Denning and Bromley, 2015)
According to the increase and decline of the absorbance of the peaks at 220 nm, each peak was manually collected and 11 peaks were obtained from the C18 reversed-phase high-performance liquid chromatography (RP-HPLC) as an individual peak to be tested for the antifungal activity against Aspergillus species
Summary
In the past two decades, there has been an increase in the prevalence of life-threatening fungal infections leading to high morbidity and mortality (Firacative, 2020). Among naturally occurring bioactive compounds with medicinal properties, antimicrobial peptides (AMPs) raised increasing attention due to their potent antimicrobial activity and simple structure (Cruz et al, 2014) In this context, antifungal peptides (AFPs) which originated from natural sources such as plants and microorganisms gained increasing attention as therapeutic agents in recent years owing to several advantages, including high selectivity and effectiveness, low immunogenicity, and good penetration to host organs and tissues (Denning and Bromley, 2015). Plants produce a large variety of AFPs that have the potential to be used in the development of novel antifungal therapeutics (Campos et al, 2018) These peptides are cysteine-rich and commonly found in seeds and, based on amino acid sequence homology, comprise a number of classes (De Lucca, 2000). We isolated and characterized a novel AFP from C. carvi seeds with an ahelix and random coil structure which showed strong antifungal activity against human and animal pathogenic Aspergillus species, while it has no obvious cytotoxicity against human red blood cells and the HEK293 cell line in vitro
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