Zirconium(IV) containing organic frameworks as a novel class of artificial proteases: Selective hydrolysis and molecular interaction studies

Selective hydrolytic cleavage of the peptide bond in proteins is one of the most important procedures in analytical biochemistry and biotechnology applications. However, this is a challenging task due to the extreme inertness of peptide bond. Commonly used natural proteases are expensive and operate only in a narrow temperature and pH range. They often suffer from self-digestion and often have limited selectivity. Therefore, new, efficient, and selective cleaving agents that are sufficiently active at non-denaturing pH and temperature conditions are highly needed. Several transition metal and lanthanide ions exhibit activity towards peptide bond hydrolysis due to their high Lewis acidity. However, under mildly acidic and neutral media they often form insoluble polynuclear complexes which limits their reactivity. In this project we will develop a new way of achieving hydrolysis of peptide bonds by using metal–organic frameworks (MOFs) that incorporate highly Lewis acidic Zr(IV) ions into their structures. Due to nanoscale porosity, high surface area, and good thermal stability, MOFs have great potential for a wide range of applications, especially in catalysis. The main objective of the research is to understand the reactivity and selectivity of Zr(IV)-MOFs towards protein hydrolysis in order to set the basis for their potential application in biotechnology and proteomics.