Antifungal activity from 14-helical β-peptides

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

doi:10.1021/ja064630y

Antifungal activity from 14-helical β-peptides

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

Chemistry (Twin Cities)

Research output: Contribution to journal › Article › peer-review

141 Scopus citations

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 language	English (US)
Pages (from-to)	12630-12631
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	128
Issue number	39
DOIs	https://doi.org/10.1021/ja064630y
State	Published - Oct 4 2006

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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.",

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AU - Pomerantz, William C.

AU - Weisblum, Bernard

AU - Gellman, Samuel H.

AU - Palecek, Sean P.

PY - 2006/10/4

Y1 - 2006/10/4

N2 - 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.

AB - 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.

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JO - Journal of the American Chemical Society

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Antifungal activity from 14-helical β-peptides

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