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Anticandidal activity of synthetic peptides: Mechanism of action revealed by scanning electron and fluorescence microscopies and synergism effect with nystatin
- Source :
- Journal of peptide science : an official publication of the European Peptide SocietyREFERENCES. 26(6)
- Publication Year :
- 2020
-
Abstract
- Candida albicans has emerged as a major public health problem in recent decades. The most important contributing factor is the rapid increase in resistance to conventional drugs worldwide. Synthetic antimicrobial peptides (SAMPs) have attracted substantial attention as alternatives and/or adjuvants in therapeutic treatments due to their strong activity at low concentrations without apparent toxicity. Here, two SAMPs, named Mo-CBP3 -PepI (CPAIQRCC) and Mo-CBP3 -PepII (NIQPPCRCC), are described, bioinspired by Mo-CBP3 , which is an antifungal chitin-binding protein from Moringa oleifera seeds. Furthermore, the mechanism of anticandidal activity was evaluated as well as their synergistic effects with nystatin. Both peptides induced the production of reactive oxygen species (ROS), cell wall degradation, and large pores in the C. albicans cell membrane. In addition, the peptides exhibited high potential as adjuvants because of their synergistic effects, by increasing almost 50-fold the anticandidal activity of the conventional antifungal drug nystatin. These peptides have excellent potential as new drugs and/or adjuvants to conventional drugs for treatment of clinical infections caused by C. albicans.
- Subjects :
- Nystatin
Antifungal Agents
Erythrocytes
Antimicrobial peptides
Antifungal drug
Electrons
Microbial Sensitivity Tests
010402 general chemistry
01 natural sciences
Biochemistry
Structural Biology
Drug Discovery
Candida albicans
medicine
Humans
Molecular Biology
Pharmacology
chemistry.chemical_classification
Reactive oxygen species
biology
010405 organic chemistry
Circular Dichroism
Organic Chemistry
General Medicine
biology.organism_classification
Corpus albicans
0104 chemical sciences
Mechanism of action
chemistry
Microscopy, Fluorescence
Toxicity
Microscopy, Electron, Scanning
Molecular Medicine
medicine.symptom
Peptides
medicine.drug
Subjects
Details
- ISSN :
- 10991387
- Volume :
- 26
- Issue :
- 6
- Database :
- OpenAIRE
- Journal :
- Journal of peptide science : an official publication of the European Peptide SocietyREFERENCES
- Accession number :
- edsair.doi.dedup.....3e30013c2cee83a79d415453b12e6a19