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Issue 26, 2020

Interplay between structural parameters and reactivity of Zr6-based MOFs as artificial proteases

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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.

Graphical abstract: Interplay between structural parameters and reactivity of Zr6-based MOFs as artificial proteases

Supplementary files

Article information


Submitted
15 Apr 2020
Accepted
21 May 2020
First published
22 May 2020

This article is Open Access
All publication charges for this article have been paid for by the Royal Society of Chemistry

Chem. Sci., 2020,11, 6662-6669
Article type
Edge Article

Interplay between structural parameters and reactivity of Zr6-based MOFs as artificial proteases

A. Loosen, F. de Azambuja, S. Smolders, J. Moons, C. Simms, D. De Vos and T. N. Parac-Vogt, Chem. Sci., 2020, 11, 6662 DOI: 10.1039/D0SC02136A

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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