The Evolutionary Conserved γ-Core Motif Influences the Anti-<i>Candida</i> Activity of the <i>Penicillium chrysogenum</i> Antifungal Protein PAF.

ABSTRACT: Small, cysteine-rich and cationic antimicrobial proteins (AMPs) from filamentous ascomycetes represent ideal bio-molecules for the development of next-generation antifungal therapeutics. They are promising candidates to counteract resistance development and may complement or even replace current small molecule-based antibiotics in the future. In this study, we show that a 14 amino acid (aa) long peptide (Pγ) spanning the highly conserved γ-core motif of the Penicillium chrysogenum antifungal protein (PAF) has antifungal activity against the opportunistic human pathogenic yeast Candida albicans. By substituting specific aa we elevated the positive net charge and the hydrophilicity of Pγ and created the peptide variants Pγ^var and Pγ^opt with 10-fold higher

SUBMITTER: Sonderegger C 

PROVIDER: S-EPMC6062912 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature