The self-replication of misfolded prion protein (PrP) aggregates is the major pathological event of different prion diseases, affecting mammal brains by cross-species transmission. Here, the structural modulation of PrP aggregates are reported by activated carbon materials upon near-infrared (NIR) light irradiation. Activated carbon cobalt (ACC) nanosheets are synthesized using glycerol and metal salts to utilize the charge carriers released under NIR light exposure. According to the microscopy and spectroscopy analysis results, NIR light-excited ACC nanosheets successfully dissociate the β-sheet-rich and plaque-like PrP aggregates into denatured fragments by modifying their amino acid residues. The in vitro assay results demonstrate that ACC nanosheets possess biocompatibility to neuroblastoma cells and alleviating effect against the neurotoxicity of PrP aggregates. This work suggests the first potential photodynamic platform for the future treatment of prion diseases.
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http://dx.doi.org/10.1002/smll.202405354 | DOI Listing |
Chem Commun (Camb)
January 2025
Department of Chemistry, Indian Institute of Technology, Roorkee 247667, India.
KRS-1, a biocompatible nickel(II) complex, is introduced as a potent fluorescent probe for PrP fibrillar aggregates. KRS-1 shows a 15-fold enhancement in PL intensity and detects all stages of PrP aggregation. Fluorescence microscopy confirms its efficacy in identifying PrP fibrillar aggregates in HT-22 cells.
View Article and Find Full Text PDFSmall
January 2025
Department of Materials Science and Engineering, Korea Advanced Institute of Science and Technology (KAIST), 335 Science Road, Daejeon, 34141, Republic of Korea.
The self-replication of misfolded prion protein (PrP) aggregates is the major pathological event of different prion diseases, affecting mammal brains by cross-species transmission. Here, the structural modulation of PrP aggregates are reported by activated carbon materials upon near-infrared (NIR) light irradiation. Activated carbon cobalt (ACC) nanosheets are synthesized using glycerol and metal salts to utilize the charge carriers released under NIR light exposure.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
January 2025
Department Biochemistry of Neurodegenerative Diseases, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, Bochum 44801, Germany.
Protein misfolding and aggregation are a hallmark of various neurodegenerative disorders. However, the underlying mechanisms driving protein misfolding in the cellular context are incompletely understood. Here, we show that the two-dimensional confinement imposed by a membrane anchor stabilizes the native protein conformation and suppresses liquid-liquid phase separation (LLPS) and protein aggregation.
View Article and Find Full Text PDFACS Chem Neurosci
December 2024
Department of Chemistry, Center for Research and Advanced Studies (Cinvestav), Mexico City 07360, Mexico.
Alzheimer's disease (AD) is the most common form of dementia worldwide. AD brains are characterized by the accumulation of amyloid-β peptides (Aβ) that bind Cu and have been associated with several neurotoxic mechanisms. Although the use of copper chelators to prevent the formation of Cu-Aβ complexes has been proposed as a therapeutic strategy, recent studies show that copper is an important neuromodulator that is essential for a neuroprotective mechanism mediated by Cu binding to the cellular prion protein (PrP).
View Article and Find Full Text PDFFoods
November 2024
Department of Biochemistry, Faculty of Medicine, Chiang Mai University, Chiang Mai 50200, Thailand.
Patients with transfusion-dependent β-thalassemia (TDT) with iron overload have been linked to hypercoagulability and increased platelet (PLT) activation that causes thrombosis. Green tea extract (GTE) rich in epigallocatechin-3-gallate (EGCG) exerts iron-chelating and antithrombotic properties. The study aimed to assess the effects of GTE treatment on plasma coagulation state and PLT function in vitro and in patients with TDT.
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