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Updated: Jun 3, 2025

Protein Misfolding Cyclic Amplification of Prions
Published on: November 7, 2012
NIR Light-Triggered Structural Modulation of Self-Assembled Prion Protein Aggregates
Jinhyeong Jang1,2, Yonghan Jo1, Chan Beum Park1
1Department of Materials Science and Engineering, Korea Advanced Institute of Science and Technology (KAIST), 335 Science Road, Daejeon, 34141, Republic of Korea.
Abstract:
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.

