Chiral dipeptide mimics possessing a fluoroolefin moiety: a relevant tool for conformational and medicinal studies.
The replacement of the amide bond in a peptide backbone is a promising strategy in peptidomimetic drug research. Over the various amide bond surrogates, the fluoroolefin moiety has been successfully developed as an effective mimic. Today, fluorine-containing compounds account for a large proportion of new active molecules in life sciences. The synthesis of fluoroolefin peptide mimics is not a trivial task and innovative approaches often need to be addressed, in particular for the stereocontrol of the double bond configuration and the chiral centres adjacent to the fluoroalkene. These fluorinated peptidomimetics have been synthesised and evaluated as metabolically stable and/or conformationally constrained analogs of enzyme inhibitors, and as tools for probing the function, structure, and binding process of receptors.
Couve-Bonnaire
Samuel
S
UMR CNRS 6014, ECOFH, IRCOF, INSA de Rouen, 1 rue Tesniere, F-76131, Mont-Saint-Aignan, France.
Cahard
Dominique
D
Pannecoucke
Xavier
X
D000475:Alkenes / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology*; D004151:Dipeptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology*; D018716:Molecular Mimicry; D010920:Placenta / Q000201:enzymology; D011480:Protease Inhibitors / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology*; D011487:Protein Conformation; D013237:Stereoisomerism
D000475:Alkenes; D004151:Dipeptides; D011480:Protease Inhibitors