causes wilt disease, which causes huge economic losses to a wide range of agricultural cash crops. Antifungal peptide P852 is an effective biocide. However, the mechanism of direct inhibition of pathogenic fungus needs to be explored. The proteomics and transcriptomics results showed that P852 mainly affected intracellular pathways such as glucose metabolism, amino acid metabolism, and oxidoreductase activity in . P852 disrupts the intracellular oxidative equilibrium in , and transmission electron microscopy observed mitochondrial swelling, disruption of membrane structure, and leakage of contents. Decreased mitochondrial membrane potential, mitochondrial cytochrome leakage, and reduced ATP production were also detected. These results suggest that P852 is able to simultaneously inhibit intracellular metabolism and disrupt the mitochondrial function of , exerting its inhibitory effects in multiple pathways together. The present study provides some insights into the multitargeted mechanism of fungus inhibition of antifungal lipopeptide substances produced by spp.
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http://dx.doi.org/10.1021/acs.jafc.3c07953 | DOI Listing |
Nat Commun
January 2025
Department of Respiratory Medicine, Nagasaki University Graduate School of Biomedical Sciences, Nagasaki, Japan.
Multidrug resistance in the pathogenic fungus Candida glabrata is a growing global threat. Here, we study mechanisms of multidrug resistance in this pathogen. Exposure of C.
View Article and Find Full Text PDFMol Divers
January 2025
Department of Microbiology, Maharshi Dayanand University, Rohtak, Haryana, 124001, India.
Cyclotides are a class of plant-derived cyclic peptides having a distinctive structure with a cyclic cystine knot (CCK) motif. They are stable molecules that naturally play a role in plant defense. Till date, more than 750 cyclotides have been reported among diverse plant taxa belonging to Cucurbitaceae, Violaceae, Rubiaceae, Solanaceae, and Fabaceae.
View Article and Find Full Text PDFMicroorganisms
January 2025
CIIMAR-Interdisciplinary Centre of Marine and Environmental Research, University of Porto, Terminal de Cruzeiros do Porto de Leixões, Av. General Norton de Matos, s/n, 4450-208 Porto, Portugal.
The intensification of aquaculture has escalated disease outbreaks and overuse of antibiotics, driving the global antimicrobial resistance (AMR) crisis. Antimicrobial peptides (AMPs) provide a promising alternative due to their rapid, broad-spectrum activity, low AMR risk, and additional bioactivities, including immunomodulatory, anticancer, and antifouling properties. AMPs derived from aquatic invertebrates, particularly marine-derived, are well-suited for aquaculture, offering enhanced stability in high-salinity environments.
View Article and Find Full Text PDFBiomolecules
January 2025
Institute of Biostructures and Bioimaging, Italian National Council for Research (IBB-CNR), Area di Ricerca Site and Headquarters, Via Pietro Castellino 111, 80131 Naples, Italy.
In recent years, fungal infections have emerged as a significant health concern across veterinary species, especially in livestock such as cattle, where fungal diseases can result in considerable economic losses, as well as in humans. In particular, species, notably and , are opportunistic pathogens that pose a threat to both animals and humans. This study focuses on the synthesis and antifungal evaluation of novel 9-fluorenylmethoxycarbonyl (Fmoc)-protected 1,2,4-triazolyl-α-amino acids and their dipeptides, designed to combat fungal pathogens.
View Article and Find Full Text PDFAntibiotics (Basel)
January 2025
Center for Targeted Drug Delivery, Department of Biomedical and Pharmaceutical Sciences, Chapman University School of Pharmacy, Harry and Diane Rinker Health Science Campus, Irvine, CA 92618, USA.
We have previously reported peptides composed of sequential arginine (R) residues paired with tryptophan (W) or 3,3-diphenyl-L-alanine residues (Dip), such as cyclic peptides [RW] and [R(Dip)], as antibacterial agents. Herein, we report antibacterial and antifungal activities of five linear peptides, namely ((DipR)(WR)), ((DipR)(WR)), ((DipR)(WR)), ((DipR)(WR)), and (DipR)R, and five cyclic peptides [(DipR)(WR)], [(DipR)(WR)], [(DipR)(WR)], [(DipR)(WR)], and [DipR], containing alternate positively charged R and hydrophobic W and Dip residues against fungal, Gram-positive, and Gram-negative bacterial pathogens. The minimum inhibitory concentrations (MICs) of all peptides were determined by the micro-broth dilution method against , , , , , , , , and .
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