A Thioether-Stabilized d-Proline-l-Proline-Induced ß-Hairpin Peptide of Defensin Segment Increases Its Anti-Candida albicans Ability.
Chembiochem
; 17(15): 1416-20, 2016 08 03.
Article
em En
| MEDLINE
| ID: mdl-27194395
ABSTRACT
We report a ß-hairpin dual stabilizing strategy a d-proline-l-proline (d-Pro-l-Pro) dipeptide as the nucleating turn, and a thioether tether as a side-chain linkage at a precisely designed position to stabilize the ß-hairpin. This method was used to modify the C-terminal ß-hairpin moiety of the plant defensin, pv-defensin, in order to obtain a stabilized peptide with enhanced anti-Candida albicans activity (MIC 84-3.0â
µm), high serum stability (50 % remaining after 48â
h) and low hemolysis (<10 % at 152â
µm). This modified peptide penetrated the C.â
albicans cell membrane within 5â
min and showed high activity against clinically isolated antibiotic-resistant C.â
albicans and Candida glabrata strains.
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Base de dados:
MEDLINE
Assunto principal:
Candida albicans
/
Prolina
/
Defensinas
/
Antifúngicos
Idioma:
En
Ano de publicação:
2016
Tipo de documento:
Article