Self-assembly and reassembly of high aspect ratio nanowires of trigeminal porphyrins and their manipulation using an atomic force microscope (AFM) is reported.
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Ferritin-based hybrid macromolecules experience unusual shift of stoichiometry distribution.
Int J Biol Macromol
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Research Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, 141700 Dolgoprudny, Russian Federation; Frank Laboratory of Neutron Physics, Joint Institute for Nuclear Research, Dubna, 141980, Russian Federation. Electronic address:
Article Synopsis
- Ferritin-based hybrids are large macromolecules with potential uses in drug delivery and vaccines, but their design is complicated.
- Researchers designed hybrids using ferritin from Helicobacter pylori and a Small Ubiquitin-like Modifier, discovering that their assembly was influenced by varying preparation methods.
- They developed a quantitative model to analyze how different stoichiometries affected the structure of these hybrids, revealing unexpected patterns and establishing a framework for better design of ferritin-based systems.
Prolonged self-assembly of H. pylori ferritin globules at physiological conditions.
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January 2025
Research Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, 141700, Russian Federation; Frank Laboratory of Neutron Physics, Joint Institute for Nuclear Research, Dubna, 141980, Russian Federation. Electronic address:
One of the promising drug delivery tools is ferritin, which features high stability at a wide range of conditions and protects cargo by its spherical protein shell. We studied the self-assembly into homoglobules of ferritin from H. pylori and a chimeric protein ferritin-SUMO.
View Article and Find Full Text PDFFabrication of core-shell nanostructure via novel ligand-defect reassembly strategy for efficient photocatalytic hydrogen evolution and NO removal.
J Colloid Interface Sci
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Institute of Fundamental and Frontier Sciences, University of Electronic Science and Technology of China, Chengdu 610054, China.
The core-shell structure often exhibits unique properties, resulting in superior physical and chemical performance distinct from individual component in the field of photocatalysis. However, traditional prepared methods such as template synthesis and layer-by-layer self-assembly are relatively complex. Therefore, it is necessary to explore an efficient and expedient approach.
View Article and Find Full Text PDFNanoscale exopolymer reassembly-trap mechanism determines contrasting PFOS exposure patterns in aquatic animals with different feeding habitats: A nano-visualization study.
J Hazard Mater
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Key Laboratory of Microbial Technology for Industrial Pollution Control of Zhejiang Province, College of Environment, Zhejiang University of Technology, Hangzhou, China. Electronic address:
The behavior and fate of PFOS (perfluorooctanesulfonate) in the aquatic environment have received great attention due to its high toxicity and persistence. The nanoscale supramolecular mechanisms of interaction between PFOS and ubiquitous EPS (exopolymers) remain unclear though EPS have been widely-known to influence the bioavailability of PFOS. Typically, the exposure patterns of PFOS in aquatic animals changed with the EPS-PFOS interaction are not fully understood.
View Article and Find Full Text PDFHuman ferritin nanocarriers for drug-delivery: A molecular view of the disassembly process.
Int J Biol Macromol
October 2024
Department of Chemical Sciences, University of Naples "Federico II", University of Napoli Federico II Complesso Universitario Monte Sant'Angelo, Via Cintia, 80126 Naples, Italy. Electronic address:
Ferritins are natural proteins which spontaneously self-assemble forming hollow nanocages physiologically deputed to iron storage and homeostasis. Thanks to their high stability and easy production in vitro, ferritins represent an intriguing system for nanobiotechnology. Here we investigated the mechanism of disassembly and reassembly of a human recombinant ferritin constituted by the heavy chain (hHFt) exploiting a new procedure which involves the use of minimal amounts of sodium dodecyl sulfate (SDS) and assessed its effectiveness in comparison with two commonly used protocols based on pH shift at highly acidic and alkaline values.
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