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Date
2020
Abstract
Fabrication of zeolite-like metal-organic frameworks (ZMOFs) for advanced applications such as enzyme immobilization is of great interest but represents a great synthetic challenge. Herein, we have developed a new strategy using proteins as structuredirected agents to direct the formation of new ZMOFs that can act as versatile platforms for in-situ encapsulation of proteins under ambient conditions. Notably, protein incorporation directs the formation of a ZMOF with a sodalite (sod) topology instead of a non-porous diamondoid (dia) topology under analogous synthetic conditions. An in-depth investigation into the mechanism of the encapsulation process revealed that histidine moieties in proteins played a crucial role in the observed templating effect. Modulating histidine content thereby influenced the resultant MOF product (from dia to dia + sod mixture and, ultimately, to sod MOF). Moreover, the resulting ZMOFs incorporated proteins and preserved their activity even after the stress of high temperatures and organic solvents. Specifically, biocatalysis and biopharmaceutical formulation applications are enabled. This study demonstrates the first example, to our knowledge, of proteins as structure-directed agents for new crystalline metal-organic materials and paves the way for in-situ incorporation of biomacromolecules into porous materials for multiple applications
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Description
peer-reviewed
Publisher
John Wiley & Sons, Inc.
Citation
Angewandte Chemie;132 (15), pp. 6322-6326
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Funding Information
National Natural Science Foundation of China, Tianjin Natural Science Foundation of China
Sustainable Development Goals
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Type
Article
Rights
https://creativecommons.org/licenses/by-nc-sa/1.0/
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