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Accueil du site > Équipes > Chimie Organique et Médicinale > Peptoid > Thèmes de recherche > Peptoid structure

Peptoid structure

Strategies are developed for the design of folded peptoids. The tBu side chain and triazolium-type side chains represent new approaches for constructing stable helical peptoids. These new side chains are now used for the synthesis of amphipathic peptoids with potent antimicrobial activity.


The positively charged triazolium-type side chain enables chemical diversity while enforcing the peptoid amide main chain to adopt the cis conformation. The cis conformation is primarily due to an attractive interaction arising from a backbone to side-chain n → π*Ar electronic delocalization.


The Click Triazolium Peptoid Side Chain : A Strong cis-Amide Inducer Enabling Chemical Diversity.
Caumes C., Roy O., Faure S., Taillefumier C. J. Am. Chem. Soc. 2012, 134, 9553-9556.


The very simple sterically hindered tert-butyl side chain exerts complete control over the peptoid amide geometry which only exists in the cis conformation. “All-cis” peptoids and alternating cis-trans peptoids have been constructed. The all-cis NtBu peptoid oligomers adopt a PolyProline-type I (PPI) helical conformation.


The Tert-Butyl Side Chain : A Powerful Means To Lock Peptoid Amide Bonds In The Cis Conformation.
Roy O., Caumes C., Esvan y., Didierjean C., Faure S., Taillefumier C. Org. Lett. 2013, 15, 2246-2249.