Functions fulfilled by proteins depend to a large extent on the ability of the intrinsically flexible polypeptide chain to fold correctly into well-ordered and compact tertiary structures and eventually to (self-)assemble. Multiple approaches, at the interface between biology, synthetic organic and polymer chemistries are currently being developed to elaborate synthetic systems with protein-like structures and functions. By using peptidomimetic chemistry, the general aims of our research are (i) to understand how to program molecules with the necessary information for self-ordering into complex and functional architectures, (ii) to create folded systems mimicking protein secondary structure elements (e.g. helices), (iii) to study interactions with biomolecules and to develop biomedical applications.
Our research efforts are devoted in part to Foldamer Chemistry with the creation of urea-based foldamers and their applications in molecular recognition and biology. We are also developing multimeric peptidomimetic architectures as tools to investigate activation of receptors of the tumour necrosis Factor receptor (TNFR) family, including Death receptors (DR). Finally our group is also interested in the synthesis of small heterocyclic peptide mimetics and their applications as enzyme inhibitors.