ArticleJournal of the American Chemical Society2023
Interrogating Encapsulated Protein Structure within Metal-Organic Frameworks at Elevated Temperature.
Article in Journal of the American Chemical Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 46 citations in OpenAlex.
- Direct Synthesis of High-Valence Protein@UiO-66 Composites: Linking Crystallization Pathways to Protein Encapsulation.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Encapsulation in a Bacterial Microcompartment Shell Improves Thermal Stability of a Glycolytic Enzyme.ACS synthetic biology · 2026Article
- Thermostability of tetanus toxoid vaccine encapsulated in metal-organic frameworks.Drug delivery and translational research · 2025Article
- Metal-organic framework-based delivery systems as nanovaccine for enhancing immunity against porcine circovirus type 2.Materials today. Bio · 2025Article
- Protein and peptide confinement within metal-organic materials.Chemical communications (Cambridge, England) · 2025Review
- An aggregation-induced conformation locking strategy facilitates the activation of lipase biocatalyst.Nature communications · 2025Article
- In Situ Metal-Organic Framework Growth in Serum Encapsulates and Depletes Abundant Proteins for Integrated Plasma Proteomics.ACS nano · 2025Article
- Enhanced Thermal and Storage Stability of Glucose Oxidase via Encapsulation in Chitosan-Coated Alginate and Carboxymethyl Cellulose Gel Particles.Foods (Basel, Switzerland) · 2025Article
- Amino Functionality Enables Aqueous Synthesis of Carboxylic Acid-Based MOFs at Room Temperature by Biomimetic Crystallization.Inorganic chemistry · 2024Article
- Recent progress in functional metal-organic frameworks for bio-medical application.Regenerative biomaterials · 2024Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Encapsulating biomacromolecules within metal-organic frameworks (MOFs) can confer thermostability to entrapped guests. It has been hypothesized that the confinement of guest molecules within a rigid MOF scaffold results in heightened stability of the guests, but no direct evidence of this mechanism has been shown. Here, we present a novel analytical method using small-angle X-ray scattering (SAXS) to solve the structure of bovine serum albumin (BSA) while encapsulated within two zeolitic imidazolate frameworks (ZIF-67 and ZIF-8). Our approach comprises subtracting the scaled SAXS spectrum of the ZIF from that of the biocomposite BSA@ZIF to determine the radius of gyration of encapsulated BSA through Guinier, Kratky, and pair distance distribution function analyses. While native BSA exposed to 70 °C became denatured, in situ SAXS analysis showed that encapsulated BSA retained its size and folded state at 70 °C when encapsulated within a ZIF scaffold, suggesting that entrapment within MOF cavities inhibited protein unfolding and thus denaturation. This method of SAXS analysis not only provides insight into biomolecular stabilization in MOFs but may also offer a new approach to study the structure of other conformationally labile molecules in rigid matrices.
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