Antifungal activity from 14-helical β-peptides

Amy J. Karlsson, William C. Pomerantz, Bernard Weisblum, Samuel H. Gellman, Sean P. Palecek

Research output: Contribution to journalArticle

117 Citations (Scopus)

Abstract

We have discovered that short β-peptides (9 or 10 residues) designed to adopt globally amphiphilic helical conformations display significant antifungal activity. The most promising β-peptides cause little lysis of human red blood cells at concentrations that kill Candida albicans, a common human fungal pathogen. Since fungi are eukaryotes, discrimination between fungal and human cells is a significant finding. Our β-peptides are active under assay conditions that mimic physiological ionic strength; in contrast, α-helix-forming host-defense α-peptides are inactive against C. albicans under these conditions.

Original languageEnglish (US)
Pages (from-to)12630-12631
Number of pages2
JournalJournal of the American Chemical Society
Volume128
Issue number39
DOIs
StatePublished - Oct 4 2006

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Peptides
Candida albicans
Cells
Candida
Pathogens
Ionic strength
Eukaryota
Fungi
Osmolar Concentration
Conformations
Assays
Blood
Erythrocytes

Cite this

Karlsson, A. J., Pomerantz, W. C., Weisblum, B., Gellman, S. H., & Palecek, S. P. (2006). Antifungal activity from 14-helical β-peptides. Journal of the American Chemical Society, 128(39), 12630-12631. https://doi.org/10.1021/ja064630y

Antifungal activity from 14-helical β-peptides. / Karlsson, Amy J.; Pomerantz, William C.; Weisblum, Bernard; Gellman, Samuel H.; Palecek, Sean P.

In: Journal of the American Chemical Society, Vol. 128, No. 39, 04.10.2006, p. 12630-12631.

Research output: Contribution to journalArticle

Karlsson, AJ, Pomerantz, WC, Weisblum, B, Gellman, SH & Palecek, SP 2006, 'Antifungal activity from 14-helical β-peptides', Journal of the American Chemical Society, vol. 128, no. 39, pp. 12630-12631. https://doi.org/10.1021/ja064630y
Karlsson, Amy J. ; Pomerantz, William C. ; Weisblum, Bernard ; Gellman, Samuel H. ; Palecek, Sean P. / Antifungal activity from 14-helical β-peptides. In: Journal of the American Chemical Society. 2006 ; Vol. 128, No. 39. pp. 12630-12631.
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