Candida albicans is one of the most common fungal pathogens. The risk of candidemia is substantially increased in immunocompromised patients. Antimicrobial peptides (AMPs) have been shown to exhibit antifungal activity. �-Peptides can be designed to mimic the structural features of natural AMPs. Hydrophobicity and cationic charge arranged in an amphipathic configuration play a key role in �-peptide antifungal activity. In order to determine the relationship between hydrophobicity and antifungal activity and selectivity, we screened 28 �-peptides exhibiting various extents of hydrophobicity against both C. albicans and human red blood cells. Both antifungal activity and hemolysis correlated with hydrophobicity, and selective HPLC retention times ranging from 23.4 to 25.6 min provided high activity with low hemolysis. Additionally, we showed that helical structure forming propensity affects this window of selective activity. In conclusion, our results provide new design parameters for generating �-peptide oligomers with selective antifungal activity.

Synthesis and antifungal activity of 14-helical β-peptides based on hydrophobicity screening

245th National Meeting (2013)

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