journal article·2025-02Open access

NIR Light‐Triggered Structural Modulation of Self‐Assembled Prion Protein Aggregates

Jinhyeong Jang, Yonghan Jo, Chan Beum Park

Small· Volume 21· Issue 8

Abstract

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.
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Research context

OpenAlex topics: Prion Diseases and Protein Misfolding · Infectious Encephalopathies and Encephalitis · Alcoholism and Thiamine Deficiency

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

Department of Materials Science and Engineering Korea Advanced Institute of Science and Technology (KAIST) 335 Science Road Daejeon 34141 Republic of Korea

Applied Science Research Institute Korea Advanced Institute of Science and Technology (KAIST) 335 Science Road Daejeon 34141 Republic of Korea

Funding

Ministry of Science and ICT, South Korea

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