Synthesis and testing of peptides for anti-prion activity

Shane Sellarajah, Cyrille Boussard, Tarnuna Lekishvili, David R. Brown, Ian H. Gilbert

    Research output: Contribution to journalArticle

    3 Citations (Scopus)

    Abstract

    Creutzfeldt-Jakob disease (CJD) is one of the fatal transmissible spongiform encephalopathies for which there is no known cure. The disease is associated with an abnormally folded prion protein, PrP-res, which is thought to form due to interaction between normal prion PrPC and PrP-es. Small peptides were designed to prevent this interaction. A structure-activity relationship is described for a series of peptides which were synthesised and tested for their activity against two prion disease model assays, an in vitro cellular assay and an in vitro anti-aggregation polymerisation assay. A number of peptides were found to be active at levels of 100 mu M. New libraries were synthesised in order to concentrate on discovering new, shorter peptides which could be leads for developing peptidomimetics. (C) 2008 Elsevier Masson SAS. All rights reserved.

    Original languageEnglish
    Pages (from-to)2418-2427
    Number of pages10
    JournalEuropean Journal of Medicinal Chemistry
    Volume43
    Issue number11
    DOIs
    Publication statusPublished - Nov 2008

    Keywords

    • Prion
    • Transmissible spongiform encephalopathy
    • Peptide
    • TRANSMISSIBLE SPONGIFORM ENCEPHALOPATHIES
    • CONGO RED
    • HIV PROTEINASE
    • INHIBITION
    • DISEASES
    • THERAPEUTICS
    • PRP
    • CONSEQUENCES
    • HAMSTERS
    • BINDING

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