Antifungal Activity from 14-Helical -Peptides
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- 作者：Amy J. Karlsson ; William C. Pomerantz ; Bernard Weisblum ; Samuel H. Gellman ; Sean P. Palecek
- 刊名：Journal of the American Chemical Society
- 出版年：2006
- 出版时间：October 4, 2006
- 年：2006
- 卷：128
- 期：39
- 页码：12630 - 12631
- 全文大小：41K
- 年卷期：v.128,no.39(October 4, 2006)
- ISSN：1520-5126
文摘
We have discovered that short 
-peptides (9 or 10 residues) designed to adopt globally amphiphilic helical conformations display significant antifungal activity. The most promising -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 -peptides are active under assay conditions that mimic physiological ionic strength; in contrast, 
-helix-forming host-defense -peptides are inactive against C. albicans under these conditions.
-peptides (9 or 10 residues) designed to adopt globally amphiphilic helical conformations display significant antifungal activity. The most promising -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 -peptides are active under assay conditions that mimic physiological ionic strength; in contrast, -helix-forming host-defense -peptides are inactive against C. albicans under these conditions.