Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 59, Issue 15, Pages 6263-6267Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202000299
Keywords
enzyme immobilization; metal-organic frameworks; protein structure; self-assembly; template synthesis; zeolite analogues
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Funding
- National Natural Science Foundation of China [21871153, 31800793]
- Tianjin Natural Science Foundation of China [18JCZDJC37300]
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Fabrication of zeolite-like metal-organic frameworks (ZMOFs) for advanced applications, such as enzyme immobilization, is of great interest but is a great synthetic challenge. Herein, we have developed a new strategy using proteins as structure-directed agents to direct the formation of new ZMOFs that can act as versatile platforms for the 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. Histidines in proteins play 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 ZMOF-incorporated proteins preserved their activity even after exposure to high temperatures and organic solvents, demonstrating their potential for biocatalysis and biopharmaceutical applications.
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