Résumé
Research in the foldamer area has advanced tremendously in recent years in establishing abiotic architectures, with stable and predictable folding patterns such as helices, sheets and ribbon shapes. These structures are stabilized by remote intra-strand contacts including hydrogen-bonds and stereoelectronic interactions, local conformational control or solvophobic effects. In this context, our group had explored a class of constrained heterocyclic -amino acids built around a thiazole ring, named ATCs. ATC oligomers showed high propensity to adopt a helical structure in the solid state and in organic solvents and water. The structure of the γ-peptide backbone showed low dependency on the nature of the side chains. In addition to fundamental questions of folding, the facial anisotropy of the platform ensures a perfect control of the spatial orientation of the appended functionalities essential to achieve biomedical and material applications. We present here the advances in the synthesis / structural characterization and use of ATC chemistry in the fields of antimicrobial control, cell targeting and organocatalysis.