Leveraging Isothermal Titration Calorimetry to Explore Structure–Property Relationships of Protein Immobilization in Metal–Organic Frameworks
Abstract
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.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Aug 09, 2022
- Source ID
- 10.1002/anie.202209110
Entities
People
- Fanrui Sha
- Kaikai Ma
- Kent O Kirlikovali
- Omar Farha
- Satoshi Kato
- Shengyi Su
- Timur Islamoglu
- Tzu‐Yi Tai
- Xiaoliang Wang
- Xingjie Wang
Organizations
- Defense Threat Reduction Agency
- National Science Foundation
- National Science and Technology Council
- Northwestern University
- United States Army