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Effect of sequence and structural properties on 14-helical beta-peptide activity against Candida albicans planktonic cells and biofilms.

Abstract：

:Beta-peptides (beta-amino acid oligomers) that mimic the amphiphilic, helical, and cationic properties of natural antimicrobial peptides have previously been shown to display antifungal activity against planktonic Candida albicans cells. Beta-peptides offer several advantages over conventional peptides composed of alpha-amino acid residues, including conformational stability, resistance to proteases, and activity at physiological salt concentrations. We examined sequence-activity relationships toward both planktonic C. albicans cells and C. albicans biofilms, and the results suggest a toxicity mechanism involving membrane disruption. A strategy for fluorescently labeling a beta-peptide without diminishing antifungal activity was devised; labeled beta-peptides penetrated the cell membrane and accumulated in the cytoplasm of both planktonic and biofilm-associated cells. The labeled beta-peptide was detected only in metabolically inactive cells, which suggests that beta-peptide entry is correlated with cell death. The presence of a beta-peptide at a concentration near the minimum inhibitory concentration completely prevented planktonic C. albicans cells from forming a biofilm, suggesting that beta-peptides may be useful in preventing fungal colonization and biofilm formation.

journal_name

ACS Chem Biol

journal_title

ACS chemical biology

authors

Karlsson AJ,Pomerantz WC,Neilsen KJ,Gellman SH,Palecek SP

doi

10.1021/cb900093r

subject

Has Abstract

pub_date

2009-07-17 00:00:00

pages

567-79

issue

7

eissn

1554-8929

issn

1554-8937

journal_volume

4

pub_type

杂志文章

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