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.
| Original language | English (US) |
|---|---|
| Article number | e202209110 |
| Journal | Angewandte Chemie - International Edition |
| Volume | 61 |
| Issue number | 37 |
| DOIs | |
| State | Published - Sep 12 2022 |
Funding
O.K.F gratefully acknowledges support from the Defense Threat Reduction Agency (HDTRA1-19-1-0007). T.-Y.T. gratefully acknowledges the Ministry of Science and Technology for providing financial support through the Postdoctoral Research Abroad Program (Taiwan; 110-2917-I-564-006). K.O.K. gratefully acknowledges support from the IIN Postdoctoral Fellowship and the Northwestern University International Institute for Nanotechnology. We thank the financial support of the CBC-NU Cell-free Biomanufacturing Institute funded by the U.S. Army Contracting Command Award W52P1J-21-9-3023. This work made use of the EPIC facility of Northwestern University's NUANCE Center, which has received support from the Soft and Hybrid Nanotechnology Experimental (SHyNE) Resource (NSF ECCS-2025633); the MRSEC program (NSF DMR1720139) at the Materials Research Center; the Keck Foundation; the International Institute for Nano-technology (IIN); and the State of Illinois through the IIN. This work made use of the IMSERC at Northwestern University, which has received support from the NSF (CHE-1048773 and DMR0521267); the SHyNE Resource (NSF ECCS-2025633); the State of Illinois, and the IIN. O.K.F gratefully acknowledges support from the Defense Threat Reduction Agency (HDTRA1‐19‐1‐0007). T.‐Y.T. gratefully acknowledges the Ministry of Science and Technology for providing financial support through the Postdoctoral Research Abroad Program (Taiwan; 110‐2917‐I‐564‐006). K.O.K. gratefully acknowledges support from the IIN Postdoctoral Fellowship and the Northwestern University International Institute for Nanotechnology. We thank the financial support of the CBC‐NU Cell‐free Biomanufacturing Institute funded by the U.S. Army Contracting Command Award W52P1J‐21‐9‐3023. This work made use of the EPIC facility of Northwestern University's NUANCE Center, which has received support from the Soft and Hybrid Nanotechnology Experimental (SHyNE) Resource (NSF ECCS‐2025633); the MRSEC program (NSF DMR1720139) at the Materials Research Center; the Keck Foundation; the International Institute for Nano‐technology (IIN); and the State of Illinois through the IIN. This work made use of the IMSERC at Northwestern University, which has received support from the NSF (CHE‐1048773 and DMR0521267); the SHyNE Resource (NSF ECCS‐2025633); the State of Illinois, and the IIN.
Keywords
- Isothermal Titration Calorimetry
- Metal–Organic Frameworks
- Protein Immobilization
- Thermodynamics
ASJC Scopus subject areas
- General Chemistry
- Catalysis