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J Am Chem Soc. 2004 Jun 9;126(22):6848-9.

Unexpected relationships between structure and function in alpha,beta-peptides: antimicrobial foldamers with heterogeneous backbones.

Author information

1
Department of Chemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.

Abstract

We describe our first effort to design antimicrobial alpha/beta-peptides based upon their helical folding behavior. alpha/beta-Peptide 3 (above), designed as a scrambled negative control, exhibited the most favorable activity profile, combining high antimicrobial activity with low hemolytic activity. This finding suggests that design principles focused primarily on structures that adopt globally amphiphilic structures may exclude productive possibilities from evaluation.

PMID:
15174837
DOI:
10.1021/ja048546z
[Indexed for MEDLINE]

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