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.
Claudon
Paul
P
CNRS, Institut de Biologie Moléculaire et Cellulaire, Laboratoire d'Immunologie et Chimie Thérapeutiques, 15 rue René Descartes, F-67000 Strasbourg, France.
Violette
Aude
A
Lamour
Karen
K
Decossas
Marion
M
Fournel
Sylvie
S
Heurtault
Béatrice
B
Godet
Julien
J
Mély
Yves
Y
Jamart-Grégoire
Brigitte
B
Averlant-Petit
Marie-Christine
MC
Briand
Jean-Paul
JP
Duportail
Guy
G
Monteil
Henri
H
Guichard
Gilles
G
D000577:Amides / Q000138:chemical synthesis / Q000737:chemistry; D000890:Anti-Infective Agents / Q000737:chemistry* / Q000494:pharmacology*; D002175:Candida / Q000187:drug effects; D002462:Cell Membrane / Q000737:chemistry / Q000187:drug effects; D015195:Drug Design; D004926:Escherichia coli / Q000187:drug effects; D008826:Microbial Sensitivity Tests; D016253:Microscopy, Immunoelectron; D008968:Molecular Conformation; D018716:Molecular Mimicry; D010455:Peptides / Q000737:chemistry* / Q000494:pharmacology*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011550:Pseudomonas aeruginosa / Q000187:drug effects; D013211:Staphylococcus aureus / Q000187:drug effects; D013329:Structure-Activity Relationship; D014508:Urea / Q000138:chemical synthesis / Q000737:chemistry
D000577:Amides; D000890:Anti-Infective Agents; D010455:Peptides; D014508:Urea