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Metal-Foldamer Porous Frameworks

Project description

Metal-foldamer frameworks: characterising folding and metal-directed self-assembly

Nature’s proteins are one of the most elegant examples of polymers, self-assembled into their myriad and multilevel structural architectures that enable intricately related and myriad functions. It is no surprise that proteins and large pieces of proteins, called peptides, provide inspiration for novel foldamers, polymers that fold into ordered conformation in solution. With the support of the Marie Skłodowska-Curie Actions programme, the MFPFs project will investigate novel ways to extend the metal coordination-driven assembly of promising metal-organic frameworks to become a process that integrates folding, self-assembly and metal coordination leading to metal-foldamer frameworks. It will include a focus on the factors influencing the resulting shape and catalytic property.

Objective

The design and precise construction of protein-inspired nanostructures through folding and metal-directed self-assembly is a challenging yet potentially rewarding endeavor for the development of new classes of functional materials. Peptides have been well established as flexible starting points for the construction of bioinspired architectures with a high level of sophistication and precise control over morphologies and functions. Concurrently, the power of metal coordination to drive assembly has been extensively explored to design functionally versatile metal-organic frameworks (MOFs). Yet, the synthesis of such coordination networks by a process that would combine folding, self-assembly and metal coordination in aqueous media is still partially unaccomplished. Foldamers - artificial synthetic folded oligomers - possess the advantages of structural robustness and high programmability which bodes well for their use in the construction of well-defined higher-order nanostructures. The project will move a step forward towards the design, synthesis and structural characterization of metal-foldamer porous frameworks and will focus on foldamer sequence evolution and metal variation to influence the main features of the assembly (shape and catalytic property). The applicant has been trained in peptide synthesis and has acquired a high level of expertise in the design and structural characterization of peptide-based assemblies and advanced materials. He will join and bring his expertise to a host laboratory that has pioneered the design of oligourea-based foldamers as peptide mimics. Secondment in an internationally renowned group in the chemistry of metalloenzyme active sites and the design of bio-inspired catalysts will provide the appropriate combination of knowledge required for this multidisciplinary study. This project represents a significant leap forward in the creation of a whole new range of fully synthetic and functional higher-order foldamer nanostructures.

Coordinator

UNIVERSITE DE BORDEAUX
Net EU contribution
€ 196 707,84
Address
PLACE PEY BERLAND 35
33000 Bordeaux
France

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Region
Nouvelle-Aquitaine Aquitaine Gironde
Activity type
Higher or Secondary Education Establishments
Links
Total cost
€ 196 707,84