3D Visualization of Proteins within Metal–Organic Frameworks via Ferritin‐Enabled Electron Microscopy

Dhaoui, Rakia; Cazarez, Saira L.; Xing, Li; Baghdadi, Elmira; Mulvey, Justin T.; Idris, Nehal S.; Hurst, Paul J.; Vena, M. Paula; Palma, Giuseppe Di; Patterson, Joseph P.

doi:10.1002/adfm.202312972

Cited by 5 publications

(1 citation statement)

References 68 publications

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“…Due to the low contrast of light elements in protein, electron microscopy has been combined with thermal calcination, , energy dispersive X-ray spectroscopy (EDS), , and metal-nanocluster labeling , to enable visualization of protein in composites. Recently, Patterson and co-workers successfully employed cryo-transmission electron microscopy (CryoTEM) and cryo-electron tomography (CryoET) to resolve the intrinsic metalloprotein Ferritin distribution inside zeolite-imidazole framework-8 (ZIF-8). Nevertheless, the quantifiable 3D coordinates of general enzymes and their role in maintaining biological activity remain unsolved.…”

Section: Introductionmentioning

confidence: 99%

Direct Imaging of Protein Clusters in Metal–Organic Frameworks

Liu,

Cui,

et al. 2024

J. Am. Chem. Soc.

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Protein@metal−organic frameworks (P@MOFs) prepared by coprecipitation of protein, metal ions, and organic ligands represent an effective method for protein stabilization with a wide spectrum of applications. However, the formation mechanism of P@MOFs via the coprecipitation process and the reason why proteins can retain their biological activity in the frameworks with highly concentrated metal ions remain unsettled. Here, by a combined methodology of single molecule localization microscopy and clustering analysis, we discovered that in this process enzyme molecules form clusters with metal ions and organic ligands, contributing to both the nucleation and subsequent crystal growth. We proposed that the clusters played an important role in the retention of overall enzymatic activity by sacrificing protein molecules on the cluster surface. This work offers fresh perspectives on protein behaviors in the formation of P@MOFs, inspiring future endeavors in the design and development of artificial bionanocomposites with high biological activities.

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Section: Introductionmentioning

confidence: 99%

Direct Imaging of Protein Clusters in Metal–Organic Frameworks

Liu,

Cui,

et al. 2024

J. Am. Chem. Soc.

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Unveiling the Dynamic Pathways of Metal–Organic Framework Crystallization and Nanoparticle Incorporation for Li–S Batteries

Song,

Huang,

Zhang

et al. 2024

Advanced Science

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Metal–organic frameworks (MOFs) present diverse building blocks for high‐performance materials across industries, yet their crystallization mechanisms remain incompletely understood due to gaps in nucleation and growth knowledge. In this study, MOF structural evolution is probed using in situ liquid phase transmission electron microscopy (TEM) and cryo‐TEM, unveiling a blend of classical and nonclassical pathways involving liquid–liquid phase separation, particle attachment–coalescence, and surface layer deposition. Additionally, ultrafast high‐temperature sintering (UHS) is employed to dope ultrasmall Cobalt nanoparticles (Co NPs) uniformly within nitrogen‐doped hard carbon nanocages confirmed by 3D electron tomography. Lithium–sulfur battery tests demonstrate the nanocage‐Co NP structure's exceptional capacity and cycling stability, attributed to Co NP catalytic effects due to its small size, uniform dispersion, and nanocage confinement. The findings propose a holistic framework for MOF crystallization understanding and Co NP tunability through ultrafast sintering, promising advancements in materials science and informing future MOF synthesis strategies and applications.

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Bayesian Optimization-Assisted Engineering of Formate Dehydrogenase Encapsulation in Multivariate Zeolitic Imidazolate Framework

Liang,

Zheng,

Shu

et al. 2024

Chem. Mater.

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Engineering of multivariate zeolitic imidazolate frameworks (mZIFs) offers substantial potential for optimizing enzyme encapsulation by enhancing encapsulation efficiency (EE), enzyme loading capacity (P loading ), retained enzymatic activity (REA), and protection. However, this area remains underexplored. In this study, we rationally employed three imidazolebased ligands with distinct functionalities�HeIM (2-ethylimidazole), HTz (1,2,4-triazole), and HIM (1-(2-hydroxyethyl)imidazole)�to fine-tune hydrophobicity and defect simultaneously within FDH@mZIF (FDH = formate dehydrogenase). Leveraging an iterative Bayesian optimization-assisted training-design-synthesis-measurement workflow, we efficiently identified F190 as the best FDH@mZIF, achieving EE = 89.3%, REA = 14.9%, and P loading = 30.3 wt%. This establishes F190 as the leading FDH-based biocatalyst in the literature. The optimal FDH-mZIF interactions in F190 were reflected by minimal structural perturbation of encapsulated FDH, as evidenced by the ATR-FTIR and fluorescence studies. Additionally, F190 can effectively safeguard the encapsulated FDH against thermal and proteolytic degradation and catalyze CO 2 -to-formate conversion while maintaining activity for at least five cycles without significant activity loss.

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3D Visualization of Proteins within Metal–Organic Frameworks via Ferritin‐Enabled Electron Microscopy

Cited by 5 publications

References 68 publications

Direct Imaging of Protein Clusters in Metal–Organic Frameworks

Direct Imaging of Protein Clusters in Metal–Organic Frameworks

Unveiling the Dynamic Pathways of Metal–Organic Framework Crystallization and Nanoparticle Incorporation for Li–S Batteries

Bayesian Optimization-Assisted Engineering of Formate Dehydrogenase Encapsulation in Multivariate Zeolitic Imidazolate Framework

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