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The Catestatin-Derived Peptides Are New Actors to Fight the Development of Oral Candidosis.

Authors :
Mancino D
Kharouf N
Scavello F
Hellé S
Salloum-Yared F
Mutschler A
Mathieu E
Lavalle P
Metz-Boutigue MH
Haïkel Y
Source :
International journal of molecular sciences [Int J Mol Sci] 2022 Feb 13; Vol. 23 (4). Date of Electronic Publication: 2022 Feb 13.
Publication Year :
2022

Abstract

Resistance to antifungal therapy of Candida albicans and non- albicans Candida strains, frequently associated with oral candidosis, is on the rise. In this context, host-defense peptides have emerged as new promising candidates to overcome antifungal resistance. Thus, the aim of this study was to assess the effectiveness against Candida species of different Catestatin-derived peptides, as well as the combined effect with serum albumin. Among Catestatin-derived peptides, the most active against sensitive and resistant strains of C . albicans , C. tropicalis and C. glabrata was the D -isomer of Cateslytin ( D -bCtl) whereas the efficiency of the L -isomer ( L -bCtl) significantly decreases against C. glabrata strains. Images obtained by transmission electron microscopy clearly demonstrated fungal membrane lysis and the leakage of the intracellular material induced by the L -bCtl and D -bCtl peptides. The possible synergistic effect of albumin on Catestatin-derived peptides activity was investigated too. Our finding showed that bovine serum albumin (BSA) when combined with the L - isomer of Catestatin ( L -bCts) had a synergistic effect against Candida albicans especially at low concentrations of BSA; however, no synergistic effect was detected when BSA interacted with L -bCtl, suggesting the importance of the C-terminal end of L -bCts (GPGLQL) for the interaction with BSA. In this context in vitro D -bCtl, as well as the combination of BSA with L -bCts are potential candidates for the development of new antifungal drugs for the treatment of oral candidosis due to Candida and non- Candida albicans , without detrimental side effects.

Details

Language :
English
ISSN :
1422-0067
Volume :
23
Issue :
4
Database :
MEDLINE
Journal :
International journal of molecular sciences
Publication Type :
Academic Journal
Accession number :
35216181
Full Text :
https://doi.org/10.3390/ijms23042066