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Updated: Jun 10, 2026
08:05
Microtensiometer for Confocal Microscopy Visualization of Dynamic Interfaces
Published on: September 9, 2022
Mechanistic Understanding of Protein-MOF Integration Through Surfactant-Driven Interfacial Design
Ehsan Rashidniyaghi1, Mohammad Khavani1, Carlie Coerver1
1Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, Texas, USA.
Summary
We developed a surfactant strategy to improve protein encapsulation in metal-organic frameworks (MOFs). This interfacial design enhances protein stability and function for applications in biocatalysis and drug delivery.
Area of Science:
- Materials Science
- Biochemistry
- Chemical Engineering
Background:
- Protein@MOF integration stabilizes proteins for materials and biomedical uses.
- Understanding protein-MOF interactions is crucial for controlling material properties.
Purpose of the Study:
- To develop a surfactant-guided strategy for protein@MOF assembly.
- To investigate the role of interfacial design in protein encapsulation and function.
Main Methods:
- Utilized lipid-based non-ionic surfactants (e.g., glycerol monooleate) to modulate protein-MOF interfaces.
- Employed all-atom molecular dynamics simulations to study surfactant-protein interactions.
- Quantified changes in encapsulation efficiency, MOF growth, and enzyme activity (kcat).
Main Results:
- Surfactants enhance protein encapsulation by 20% and accelerate MOF growth by 30%.
- Lecithin incorporation improved horseradish peroxidase bioactivity up to six-fold and kcat by 60-fold.
- Molecular dynamics revealed concentration-dependent, domain-specific surfactant-protein interactions.
Conclusions:
- Surfactant-driven interfacial design is a general strategy to boost protein@MOF stability and function.
- This approach offers alternatives to lipid nanodiscs for membrane protein stabilization.
- Enables advancements in biocatalysis, biosensing, and drug delivery applications.
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