Molecular insight into interactions between MOF-based nanozymes and biomolecules using x-ray absorption fine structure (XAFS) spectroscopy

The hydrolysis of proteins is a challenging task due to the inertness of the peptide bond, yet it is crucial for many applications in biotechnology and proteomics. Nanozymes, i.e., nano-engineered materials that function as artificial enzymes, can promote protein fragmentation and overcome some of the key issues associated with proteolytic enzymes, such as high cost and low stability. Metal-organic frameworks (MOFs) based on Zr and Ce metals have attracted attention due to their excellent catalytic activity, also towards complex biomolecules such as proteins. However, the mode of interactions between the proteins and the MOFs is still poorly understood, despite being essential for developing these MOFs as the next generation of nanozymes for protein hydrolysis. Within this context, the present proposal aims to provide detailed insight into the molecular interactions occurring between proteins and MOF’s pores and its catalytic sites, moving from discrete water-soluble {M6O8} metal-oxo clusters, which are the building blocks of the MOFs, to a two-dimensional {M6O8}-based coordination polymer, and finally to {M6O8}-based three-dimensional MOFs. Various in-house and synchrotron-based techniques will be combined to investigate the molecular interactions, as well as the redox activity of the catalytic site and the local structure modifications of the {M6O8}-clusters, advancing further the emerging field of artificial enzymatic catalysis.