Abstract
Structural parameters influencing the reactivity of metal–organic frameworks (MOF) are challenging to establish. However, understanding their effect is crucial to further develop their catalytic potential. Here, we uncovered a correlation between reaction kinetics and the morphological structure of MOF-nanozymes using the hydrolysis of a dipeptide under physiological pH as model reaction. Comparison of the activation parameters in the presence of NU-1000 with those observed with MOF-808 revealed the reaction outcome is largely governed by the Zr6 cluster. Additionally, its structural environment completely changes the energy profile of the hydrolysis step, resulting in a higher energy barrier ΔG‡ for NU-1000 due to a much larger ΔS‡ term. The reactivity of NU-1000 towards a hen egg white lysozyme protein under physiological pH was also evaluated, and the results pointed to a selective cleavage at only 3 peptide bonds. This showcases the potential of Zr-MOFs to be developed into heterogeneous catalysts for non-enzymatic but selective transformation of biomolecules, which are crucial for many modern applications in biotechnology and proteomics.
Highlights
Selective hydrolytic cleavage of peptide bonds is key to many chemical and biological applications such as the study of protein function,[1] the analysis of protein folding,[2] proteomics,[3] and the mapping of enzyme active sites.[4,5,6] Proteolytic enzymes or peptidases commonly used for this purpose, e.g., trypsin, are costly, and generally afford short peptide fragments which frequently results in partial protein sequence determination.[7]
This showcases the potential of Zr-metal–organic frameworks (MOF) to be developed into heterogeneous catalysts for non-enzymatic but selective transformation of biomolecules, which are crucial for many modern applications in biotechnology and proteomics
We provided detailed analysis of kinetic, thermodynamic and structural data for NU-1000 MOF mediated hydrolysis of peptide bond. Comparing these data with the structural and thermodynamic parameters obtained for MOF808 nanozyme, allowed us to identify key parameters that in uence hydrolytic reaction catalyzed by Zr6 based MOFs
Summary
Selective hydrolytic cleavage of peptide bonds is key to many chemical and biological applications such as the study of protein function,[1] the analysis of protein folding,[2] proteomics,[3] and the mapping of enzyme active sites.[4,5,6] Proteolytic enzymes or peptidases commonly used for this purpose, e.g., trypsin, are costly, and generally afford short peptide fragments which frequently results in partial protein sequence determination.[7]. Edge Article solvents,[28,30] we decided to study other Zr-MOFs as heterogeneous arti cial proteases to correlate their structure with reactivity and, in the case of protein hydrolysis, the with selectivity of cleavage.
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