AI Article Synopsis
- Protamine peptide (PP) from salmon exhibits antifungal properties against Candida albicans, demonstrating both fungicidal effects and inhibition of hyphal development through different concentrations.
- At lethal levels, PP's action includes energy-dependent uptake leading to ATP loss and reactive oxygen species generation, while sublethal doses disrupt hyphal growth by binding to the fungus's surface.
- The modified cyclic form of PP, which maintains efficacy in high salt environments, displays even stronger antifungal activity in vitro and significantly protects mice from C. albicans infections, highlighting its therapeutic potential.
Article Abstract
Protamine peptide (PP) derived from salmon is a 14-mer with 10 arginine residues. We investigated the in vitro and in vivo antifungal activity of PP against Candida albicans PP showed a concentration-dependent dual mode of action, with fungicidal activity and inhibitory activity for hyphal development in vitro. At lethal concentrations of PP, intracellular accumulation of PP was energy-dependent but independent of endocytosis, and resulted in ATP efflux and the generation of reactive oxygen species in the cells. PP at sublethal concentrations inhibited hyphal development in C. albicans by binding to the cell surface. Though antifungal activity of PP was inactivated by high concentrations of NaCl, the antifungal activity of the synthetic cyclic (via a disulfide bond) form of PP (cyclic PP) was not. Cyclic PP also showed the concentration-dependent dual mode of action, and had five-fold greater antifungal activity than PP. The advantage of antifungal activity of cyclic PP compared with PP in vitro resulted in a high in vivo efficacy in a murine oral candidiasis model. Oral treatment with cyclic PP inhibited hyphal development of C. albicans on mouse tongues and protected against the development of severe candidiasis. This study shows the therapeutic potential of cyclic PP as an antifungal peptide against C. albicans.
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| http://dx.doi.org/10.1093/femsyr/fow099 | DOI Listing |
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