EconPapers    
Economics at your fingertips  
 

A zirconium metal-organic framework with SOC topological net for catalytic peptide bond hydrolysis

Sujing Wang (), Hong Giang T. Ly, Mohammad Wahiduzzaman, Charlotte Simms, Iurii Dovgaliuk, Antoine Tissot, Guillaume Maurin, Tatjana N. Parac-Vogt () and Christian Serre ()
Additional contact information
Sujing Wang: Institut des Matériaux Poreux de Paris, Ecole Normale Supérieure, ESPCI Paris, CNRS, PSL Université
Hong Giang T. Ly: KU Leuven
Mohammad Wahiduzzaman: ICGM, Univ. Montpellier, CNRS, ENSCM
Charlotte Simms: KU Leuven
Iurii Dovgaliuk: Institut des Matériaux Poreux de Paris, Ecole Normale Supérieure, ESPCI Paris, CNRS, PSL Université
Antoine Tissot: Institut des Matériaux Poreux de Paris, Ecole Normale Supérieure, ESPCI Paris, CNRS, PSL Université
Guillaume Maurin: ICGM, Univ. Montpellier, CNRS, ENSCM
Tatjana N. Parac-Vogt: KU Leuven
Christian Serre: Institut des Matériaux Poreux de Paris, Ecole Normale Supérieure, ESPCI Paris, CNRS, PSL Université

Nature Communications, 2022, vol. 13, issue 1, 1-8

Abstract: 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.

Date: 2022
References: View references in EconPapers View complete reference list from CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
https://www.nature.com/articles/s41467-022-28886-5 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-28886-5

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-022-28886-5

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().

 
Page updated 2025-03-19
Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-28886-5