Leveraging Isothermal Titration Calorimetry to Explore Structure-Property Relationships of Protein Immobilization in Metal-Organic Frameworks.
Isothermal Titration Calorimetry
Metal-Organic Frameworks
Protein Immobilization
Thermodynamics
Journal
Angewandte Chemie (International ed. in English)
ISSN: 1521-3773
Titre abrégé: Angew Chem Int Ed Engl
Pays: Germany
ID NLM: 0370543
Informations de publication
Date de publication:
12 09 2022
12 09 2022
Historique:
received:
21
06
2022
pubmed:
23
7
2022
medline:
9
9
2022
entrez:
22
7
2022
Statut:
ppublish
Résumé
Proteins immobilized in metal-organic frameworks (MOFs) often show extraordinary stability. However, most efforts to immobilize proteins in MOFs have only been exploratory. Herein, we present the first systematic study on the thermodynamics of protein immobilization in MOFs. Using insulin as a probe, we leveraged isothermal titration calorimetry (ITC) to investigate how topology, pore size, and hydrophobicity of MOFs influence immobilization. ITC data obtained from the encapsulation of insulin in a series of Zr-MOFs reveals that MOFs provide proteins with a hydrophobic stabilizing microenvironment, making the encapsulation entropically driven. In particular, the pyrene-based NU-1000 tightly encapsulates insulin in its ideally sized mesopores and stabilizes insulin through π-π stacking interactions, resulting in the most enthalpically favored encapsulation process among this series. This study reveals critical insights into the structure-property relationships of protein immobilization.
Identifiants
pubmed: 35867849
doi: 10.1002/anie.202209110
doi:
Substances chimiques
Insulins
0
Metal-Organic Frameworks
0
Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
e202209110Informations de copyright
© 2022 Wiley-VCH GmbH.
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