ArticleChemistry of materials : a publication of the American Chemical Society2022
Role of Molecular Modification and Protein Folding in the Nucleation and Growth of Protein-Metal-Organic Frameworks.
Article in Chemistry of materials : a publication of the American Chemical Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 32 citations in OpenAlex.
- Zeolitic Imidazolate Frameworks Allows for the Thermal Stabilization of Live Viral Vaccine in the Absence of Lyophilization.ACS omega · 2025Article
- Mechanistic Understanding of Protein-MOF Integration through Surfactant-Driven Interfacial Design.bioRxiv : the preprint server for biology · 2025Article
- One-Pot Encapsulation of Enzymes in a Calcium Carboxylate Metal-Organic Framework for Improved Buffer Stability.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Photosystem I and ZIF-8 Interfacing: Entrapment and Immobilization.Inorganic chemistry · 2025Article
- In Situ Metal-Organic Framework Growth in Serum Encapsulates and Depletes Abundant Proteins for Integrated Plasma Proteomics.ACS nano · 2025Article
- Closing the Loop in the Carbon Cycle: Enzymatic Reactions Housed in Metal-Organic Frameworks for COApplied biochemistry and biotechnology · 2025Review
- Machine Learning Optimizing Enzyme/ZIF Biocomposites for Enhanced Encapsulation Efficiency and Bioactivity.JACS Au · 2024Article
- Metallo-β-lactamases immobilized by magnetic zeolitic imidazolate frameworks-8 for degradation of β-lactam antibiotics in an aqueous environment.RSC advances · 2023Article
- Tuning Immobilized Enzyme Features by Combining Solid-Phase Physicochemical Modification and Mineralization.International journal of molecular sciences · 2022Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Metal-organic frameworks (MOFs) are a class of porous nanomaterials that have been extensively studied as enzyme immobilization substrates. During in situ immobilization, MOF nucleation is driven by biomolecules with low isoelectric points. Investigation of how biomolecules control MOF self-assembly mechanisms on the molecular level is key to designing nanomaterials with desired physical and chemical properties. Here, we demonstrate how molecular modifications of bovine serum albumin (BSA) with fluorescein isothiocyanate (FITC) can affect MOF crystal size, morphology, and encapsulation efficiency. Final crystal properties are characterized using scanning electron microscopy (SEM), powder X-ray diffraction (PXRD), fluorescent microscopy, and fluorescence spectroscopy. To probe MOF self-assembly, in situ experiments were performed using cryogenic transmission electron microscopy (cryo-TEM) and X-ray diffraction (XRD). Biophysical characterization of BSA and FITC-BSA was performed using ζ potential, mass spectrometry, circular dichroism studies, fluorescence spectroscopy, and Fourier transform infrared (FTIR) spectroscopy. The combined data reveal that protein folding and stability within amorphous precursors are contributing factors in the rate, extent, and mechanism of crystallization. Thus, our results suggest molecular modifications as promising methods for fine-tuning protein@MOFs' nucleation and growth.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.