Doctoral enrollment, Design and synthesis of foldamer-based enzyme mimetics, institute European chemistry and biology (IECB) Guichard

In Nature, folding and function of biopolymers, such as proteins or nucleic acids, are two closely related notions that lead to an impressive variety of biological processes to occur. The design of bioinspired architectures to create innovative and functional nano(bio)systems in aqueous 

media has been a longstanding goal of the scientific community. Access to artificial enzymatic systems that would lead to efficient and new biocatalysts is of particular interest. Synthetic sequence-specific folded oligomers (also called “foldamers”) possess interesting features to create self-assembled protein-like frameworks, with topologies similar to and beyond those of natural polypeptides. The ability of some foldamer backbones to form predictable and well-defined secondary structures, with helical folding properties being independent from the nature of the side-chain used (i.e. primary sequence), should facilitate morphological control at the nano-scale while displaying the desired functionalities. However, attempts to reproduce enzymatic activities using foldamer chemistry have remained limited thus far.

Our group has pioneered the development and the structural characterization of aliphatic oligoureas as a new class of peptidomimetic foldamers during the last decade. The remarkable compatibility of their backbones with alpha-peptides has been recently demonstrated, highlighting thus the potential of interfacing natural peptides and urea based backbones to create chimeric structures. Thus, this PhD project aims

to engineer de novo enzyme-like architectures using supramolecular assemblies of water-soluble peptide-oligourea chimera. 

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