Unexpected relationships between structure and function in alpha,beta-peptides: antimicrobial foldamers with heterogeneous backbones.
Unexpected relationships between structure and function in alpha,beta-peptides: antimicrobial foldamers with heterogeneous backbones. Research Abstract Details
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.
Unexpected relationships between structure and function in alpha,beta-peptides: antimicrobial foldamers with heterogeneous backbones. Publishing Authors By Initials
Unexpected relationships between structure and function in alpha,beta-peptides: antimicrobial foldamers with heterogeneous backbones. Journal Published:
PUBLICATION TYPE: Research Support, U.S. Gov't,
Journal: Journal of the American Chemical Society
VOLUME: 126
Page Numbers: 6848-9
Journal Abbreviation: J. Am. Chem. Soc.
ISSN: 0002-7863
DAY: 9
MONTH: Jun
YEAR: 2004
Unexpected relationships between structure and function in alpha,beta-peptides: antimicrobial foldamers with heterogeneous backbones. Information
Number of References:
LANGUAGE: eng
NlmUniqueID: 7503056
Unexpected relationships between structure and function in alpha,beta-peptides: antimicrobial foldamers with heterogeneous backbones. Keywords Mesh Terms:
KEYWORDS: Structure-Activity Relationship
MESH TERMS: drug effects
Chemical & Substance for Abstract: Unexpected relationships between structure and function in alpha,beta-peptides: antimicrobial foldamers with heterogeneous backbones. Information
Substance Name: Peptides
Registry Number: 0
Grant and Affiliation Information for Unexpected relationships between structure and function in alpha,beta-peptides: antimicrobial foldamers with heterogeneous backbones.
AFFILIATION: Department of Chemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.
Country: United States
AGENCY: United States NIGMS
GRANT: GM08293-14
ACRONYM: GM
MEDLINETA: J Am Chem Soc
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