Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Amyloid Fibrils

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Principles, Materials, and Devices for Solar-to-Chemical Biotransformation.

Chemical reviews·2026

Same author

Nanoarchitectonic Semiconductor-Bio Hybrid Systems with Enhanced Charge Transfer for Hydrogen Peroxide Production.

Journal of the American Chemical Society·2026

Same author

Scalable Hygroscopic Moisture-Electric Generator With Long-Term Stability for Self-Powered Wound-Healing Stimulation.

Advanced materials (Deerfield Beach, Fla.)·2026

Same author

Fallen-leaf-sensitized biosolar oxygenation of hydrocarbons.

Green chemistry : an international journal and green chemistry resource : GC·2026

Same author

A hierarchical shell locks and stabilizes perovskite nanocrystals with near-unity quantum yield.

Science (New York, N.Y.)·2026

Same author

Nanodiamonds in Advancing Biomedical Sciences.

ACS applied materials & interfaces·2025

Search research articles

Related Experiment Video

Updated: Jun 3, 2025

Protein Misfolding Cyclic Amplification of Prions

Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

NIR Light-Triggered Structural Modulation of Self-Assembled Prion Protein Aggregates.

Jinhyeong Jang^1,2, 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.

Small (Weinheim an Der Bergstrasse, Germany)

|January 6, 2025

Summary

Activated carbon cobalt (ACC) nanosheets, when exposed to near-infrared light, can break down misfolded prion protein (PrP) aggregates. This novel photodynamic approach shows promise for treating prion diseases and protecting brain cells.

Keywords:

activated carbon near‐infrared light prion protein self‐assembly

More Related Videos

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

Monitoring Cell-to-cell Transmission of Prion-like Protein Aggregates in Drosophila Melanogaster

Monitoring Cell-to-cell Transmission of Prion-like Protein Aggregates in Drosophila Melanogaster

Published on: March 12, 2018

Related Experiment Videos

Last Updated: Jun 3, 2025

Protein Misfolding Cyclic Amplification of Prions

Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

Monitoring Cell-to-cell Transmission of Prion-like Protein Aggregates in Drosophila Melanogaster

Monitoring Cell-to-cell Transmission of Prion-like Protein Aggregates in Drosophila Melanogaster

Published on: March 12, 2018

Area of Science:

Biochemistry
Materials Science
Neuroscience

Background:

Prion diseases are characterized by misfolded prion protein (PrP) aggregate self-replication, impacting mammalian brains.
Cross-species transmission poses a significant challenge in understanding and treating these neurodegenerative conditions.

Purpose of the Study:

To investigate the structural modulation of prion protein (PrP) aggregates using activated carbon materials.
To explore the potential of near-infrared (NIR) light-activated materials for treating prion diseases.

Main Methods:

Synthesis of activated carbon cobalt (ACC) nanosheets using glycerol and metal salts.
Utilizing charge carriers released from ACC nanosheets under NIR light exposure.
Employing microscopy and spectroscopy for structural analysis of PrP aggregates and ACC nanosheets.

Main Results:

NIR light-excited ACC nanosheets effectively dissociated beta-sheet-rich, plaque-like PrP aggregates into denatured fragments.
Modification of PrP amino acid residues was observed following ACC nanosheet treatment.
In vitro assays confirmed ACC nanosheets' biocompatibility with neuroblastoma cells and their neuroprotective effects against PrP toxicity.

Conclusions:

Activated carbon cobalt (ACC) nanosheets represent a novel photodynamic platform for modulating PrP aggregates.
This approach demonstrates potential for future therapeutic strategies against prion diseases.
The study highlights the efficacy of NIR light-activated materials in addressing neurotoxicity associated with misfolded proteins.