Therapeutic approaches against common structural features of toxic oligomers shared by multiple amyloidogenic proteins

Marcos J. Guerrero-Muñoz, Diana L. Castillo-Carranza, Rakez Kayed

    Research output: Contribution to journalReview articlepeer-review

    89 Scopus citations

    Abstract

    Impaired proteostasis is one of the main features of all amyloid diseases, which are associated with the formation of insoluble aggregates from amyloidogenic proteins. The aggregation process can be caused by overproduction or poor clearance of these proteins. However, numerous reports suggest that amyloid oligomers are the most toxic species, rather than insoluble fibrillar material, in Alzheimer's, Parkinson's, and Prion diseases, among others. Although the exact protein that aggregates varies between amyloid disorders, they all share common structural features that can be used as therapeutic targets. In this review, we focus on therapeutic approaches against shared features of toxic oligomeric structures and future directions.

    Original languageEnglish (US)
    Pages (from-to)468-478
    Number of pages11
    JournalBiochemical Pharmacology
    Volume88
    Issue number4
    DOIs
    StatePublished - Apr 15 2014

    Keywords

    • Amyloid oligomers
    • Anti-amyloid small molecules
    • Immunotherapy

    ASJC Scopus subject areas

    • Biochemistry
    • Pharmacology

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