Mechanistic Understanding of Protein-MOF Integration through Surfactant-Driven Interfacial Design.

Area of Science:

• Materials Science
• Biomedical Science
• Biotechnology

Background:

• Protein stabilization using metal-organic frameworks (Protein@MOF) is crucial for material and biomedical applications.
• The molecular mechanisms governing protein-MOF interactions are not fully understood, limiting optimization of Protein@MOF systems.
• Current methods lack a general platform for systematically investigating these interactions.

Purpose of the Study:

• To develop a general platform for investigating protein-MOF interactions.
• To elucidate the role of interfacial design in modulating Protein@MOF assembly and stability.
• To explore surfactant-guided strategies for enhancing Protein@MOF properties.

Main Methods:

• A surfactant-guided strategy was developed to modulate Protein@MOF assembly.
• Lipid-based non-ionic surfactants, specifically glycerol monooleate (GMO), were employed.
• All-atom molecular dynamics simulations were used to analyze molecular interactions.

Main Results:

• The interfacial environment significantly impacts encapsulation efficiency, structural retention, and functional performance of Protein@MOF.
• GMO increased protein encapsulation by 20% and MOF growth rate by 30%.
• Molecular dynamics simulations revealed concentration-dependent, domain-specific interactions between GMO and protein surface residues.

Conclusions:

• Surfactant-driven interfacial design offers a powerful approach to fine-tune Protein@MOF stability and performance.
• This strategy provides molecular insights into protein-MOF interactions, paving the way for improved protein stabilization.
• The findings support the development of Protein@MOF as alternatives to lipid nanodiscs and for applications in drug delivery, biocatalysis, and biosensing.