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Fluorescent non-canonical amino acid as a site-specific conformational probe of prion formation.

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Generation of Infectious Prions Amenable to Site-specific Click Chemistry.

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Updated: Jun 11, 2026

High-throughput Screening for Protein-based Inheritance in S. cerevisiae
08:12

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Published on: August 8, 2017

Generation of Infectious Prions Amenable to Site-Specific Click Chemistry.

Ryan G Campbell, Jolene N Iseler, Abigail M Schwind

    ACS Chemical Biology
    |June 9, 2026
    PubMed
    Summary

    Researchers developed a new method to study prion diseases by modifying a key protein. This technique allows for the creation of various labeled prions, aiding in understanding prion infectivity and disease mechanisms.

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    Published on: August 19, 2012

    Protein Misfolding Cyclic Amplification of Prions
    10:12

    Protein Misfolding Cyclic Amplification of Prions

    Published on: November 7, 2012

    Area of Science:

    • Neuroscience
    • Biochemistry
    • Molecular Biology

    Background:

    • Prion diseases are fatal neurodegenerative conditions.
    • They involve the misfolding of the prion protein (PrPC) into an infectious form (PrPSc).
    • Studying PrPSc is challenging due to difficulties in producing and modifying functional molecules.

    Purpose of the Study:

    • To overcome limitations in studying PrPSc biology.
    • To develop a method for direct investigation of PrPSc structure and function.
    • To enable the creation of selectively modified prions for research.

    Main Methods:

    • Site-specific substitution of tryptophan residue 99 in PrPC with p-azido-l-phenylalanine (AzF).
    • Utilizing click chemistry for modification of the AzF-substituted prion.
    • In vitro propagation of infectious and non-infectious PrPSc conformers using the modified substrate.

    Main Results:

    • The W99AzF PrPC substrate successfully propagated PrPSc conformers in vitro.
    • The W99AzF PrPSc retained reactivity to click chemistry after conversion.
    • This enabled the production of various modified prions.

    Conclusions:

    • The developed method allows for the direct study of PrPSc biology.
    • Click chemistry-compatible, modified prions can be generated.
    • This approach facilitates targeted investigations into prion infectivity and disease mechanisms.