Inhibiting toxic aggregation of amyloidogenic proteins: A therapeutic strategy for protein misfolding diseases

Biao Cheng, Hao Gong, Hongwen Xiao, Robert B. Petersen, Ling Zheng, Kun Huang

Research output: Contribution to journalReview articlepeer-review

165 Scopus citations


Background The deposition of self-assembled amyloidogenic proteins is associated with multiple diseases, including Alzheimer's disease, Parkinson's disease and type 2 diabetes mellitus. The toxic misfolding and self-assembling of amyloidogenic proteins are believed to underlie protein misfolding diseases. Novel drug candidates targeting self-assembled amyloidogenic proteins represent a potential therapeutic approach for protein misfolding diseases. Scope of review In this perspective review, we provide an overview of the recent progress in identifying inhibitors that block the aggregation of amyloidogenic proteins and the clinical applications thereof. Major conclusions Compounds such as polyphenols, certain short peptides, and monomer- or oligomer-specific antibodies, can interfere with the self-assembly of amyloidogenic proteins, prevent the formation of oligomers, amyloid fibrils and the consequent cytotoxicity. General significance Some inhibitors have been tested in clinical trials for treating protein misfolding diseases. Inhibitors that target the aggregation of amyloidogenic proteins bring new hope to therapy for protein misfolding diseases.

Original languageEnglish
Pages (from-to)4860-4871
Number of pages12
JournalBBA - General Subjects
Issue number10
StatePublished - 2013


  • Amyloid
  • Cytotoxicity
  • Inhibitor
  • Polyphenols
  • Protein misfolding disease


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