ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2026
Mechanistic Understanding of Protein-MOF Integration Through Surfactant-Driven Interfacial Design.
Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed.
- Encapsulation in a Bacterial Microcompartment Shell Improves Thermal Stability of a Glycolytic Enzyme.ACS synthetic biology · 2026Article
- Lipid-Metal-Organic Framework Colloidosomes for Multimodal Encapsulation and Pollutant Capture.Computational and structural biotechnology journal · 2026Article
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Abstract
Integration of proteins into metal-organic frameworks (Protein@MOF) offers an effective strategy for protein stabilization across materials and biomedical applications. However, the molecular mechanism of protein-MOF interactions remains poorly understood, limiting rational control over their chemical and physical properties. Here, we develop a surfactant-guided strategy to modulate the assembly of protein@MOF through interfacial design. We discovered that the interfacial environment between proteins and MOFs is the dominant factor controlling encapsulation efficiency, structural integrity, and functional performance. Lipid-based non-ionic surfactants such as glycerol monooleate (GMO) increase the protein's solvent-accessible surface area (SASA), suggesting partial remodeling of the protein surface and hydration shell. Interfacial GMO enhances protein encapsulation by 20% and accelerates MOF growth by 30%. Importantly, for horseradish peroxidase (HRP) encapsulated in MOF, incorporation of lecithin results in up to a six-fold enhancement in retained bioactivity and a near 60-fold increase in k
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