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Consequences of isostructural main-chain modifications for the design of antimicrobial foldamers: helical mimics of host-defense peptides based on a heterogeneous amide/urea backbone.

TitreConsequences of isostructural main-chain modifications for the design of antimicrobial foldamers: helical mimics of host-defense peptides based on a heterogeneous amide/urea backbone.
Publication TypeJournal Article
Year of Publication2010
AuthorsClaudon, P, Violette, A, Lamour, K, Decossas, M, Fournel, S, Heurtault, B, Godet, J, Mély, Y, Jamart-Grégoire, B, Averlant-Petit, M-C, Briand, J-P, Duportail, G, Monteil, H, Guichard, G
JournalAngew Chem Int Ed Engl
Volume49
Issue2
Pagination333-6
Date Published2010
ISSN1521-3773
Mots-clésAmides, Anti-Infective Agents, Candida, Cell Membrane, Drug Design, Escherichia coli, Microbial Sensitivity Tests, Microscopy, Immunoelectron, Molecular Conformation, Molecular Mimicry, Peptides, Protein Folding, Protein Structure, Secondary, Pseudomonas aeruginosa, Staphylococcus aureus, Structure-Activity Relationship, Urea
DOI10.1002/anie.200905591
Alternate JournalAngew. Chem. Int. Ed. Engl.
PubMed ID19957258