Structure-activity studies of 14-helical antimicrobial β-peptides: probing the relationship between conformational stability and antimicrobial potency

…, EA Porter, B Weisblum, SH Gellman

Index: Raguse, Tami L.; Porter, Emilie A.; Weisblum, Bernard; Gellman, Samuel H. Journal of the American Chemical Society, 2002 , vol. 124, # 43 p. 12774 - 12785

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Citation Number: 236

Abstract

Antimicrobial α-helical α-peptides are part of the host-defense mechanism of multicellular organisms and could find therapeutic use against bacteria that are resistant to conventional antibiotics. Recent work from Hamuro et al. has shown that oligomers of β-amino acids (“β- peptides”) that can adopt an amphiphilic helix defined by 14-membered ring hydrogen bonds (“14-helix”) are active against Escherichia coli [Hamuro, Y.; Schneider, JP; ...