Abstract
The discovery of nanozymes for selective fragmentation of proteins would boost the emerging areas of modern proteomics, however, the development of efficient and reusable artificial catalysts for peptide bond hydrolysis is challenging. Here we report the catalytic properties of a zirconium metal-organic framework, MIP-201, in promoting peptide bond hydrolysis in a simple dipeptide, as well as in horse-heart myoglobin (Mb) protein that consists of 153 amino acids. We demonstrate that MIP-201 features excellent catalytic activity and selectivity, good tolerance toward reaction conditions covering a wide range of pH values, and importantly, exceptional recycling ability associated with easy regeneration process. Taking into account the catalytic performance of MIP-201 and its other advantages such as 6-connected Zr6 cluster active sites, the green, scalable and cost-effective synthesis, and good chemical and architectural stability, our findings suggest that MIP-201 may be a promising and practical alternative to commercially available catalysts for peptide bond hydrolysis.
Highlights
The discovery of nanozymes for selective fragmentation of proteins would boost the emerging areas of modern proteomics, the development of efficient and reusable artificial catalysts for peptide bond hydrolysis is challenging
Unlike the large number of Zr–metal–organic frameworks (MOFs) based on high connection-number building units, very few Zr–MOFs are constructed from 6-connected Zr6-oxo clusters, including PCN-22422, PCN-77723 (PCN, Porous Coordination Network), UMCM-30924 (UMCM, University of Michigan Crystalline Material), the interpenetrated Zr–BTB25, MOF-80819, and BUT-108 (BUT, Beijing University of Technology)[26]
The trigonal prismatic configuration of the 6-connected Zr6-oxo cluster is of a particular interest for the design of new topological structure of Zr–MOFs27, since it has shown similar functions as trimer-building units of trivalent metal ions in the MOF-framework fabrication, such as the case of PCN-777 to be related to the metal(III) oxo-trimer-based MIL100 and MIL-101 (MIL, Materials of Institut Lavoisier)[23]
Summary
The discovery of nanozymes for selective fragmentation of proteins would boost the emerging areas of modern proteomics, the development of efficient and reusable artificial catalysts for peptide bond hydrolysis is challenging. We present the first Zr–MOF with square–octahedron (soc) topological net constructed from Zr6-oxo cluster secondary building units (SBUs) and a tetracarboxylate linker (3,3,5,5′-tetracarboxydiphenylmethane (H4mdip)), denoted as MIP-201 (MIP, materials of the Institute of Porous Materials from Paris), that addresses the challenge of developing a highly efficient and robust heterogeneous catalyst for peptide-bond hydrolysis.
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