title: Unexpected relationships between structure and function in alpha,beta-peptides: antimicrobial foldamers with heterogeneous backbones.
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.
authors.affiliation: Department of Chemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.
authors.forename: Margaret A
authors.initials: MA
authors.lastname: Schmitt
authors.forename: Bernard
authors.initials: B
authors.lastname: Weisblum
authors.forename: Samuel H
authors.initials: SH
authors.lastname: Gellman
mesh_terms: D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000494:pharmacology*; D002851:Chromatography, High Pressure Liquid; D006090:Gram-Negative Bacteria / Q000187:drug effects; D006461:Hemolysis / Q000187:drug effects; D006801:Humans; D006860:Hydrogen Bonding; D015394:Molecular Structure; D010455:Peptides; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship
chemical_list: D000900:Anti-Bacterial Agents; D010455:Peptides