Observation of reduced cytotoxicity of aggregated amyloidogenic peptides with chaperone-like molecules

Lei Liu, Lan Zhang, Lin Niu, Meng Xu, Xiaobo Mao, Yanlian Yang, Chen Wang

Research output: Contribution to journalArticlepeer-review

37 Scopus citations


The pathogenesis of many neurodegenerative diseases is associated with different types of aggregates of amyloidogenic peptides, including senile plaques, fibrils, protofibrils, and oligomers. It is therefore valuable to explore diversity of approaches toward reducing the cytotoxicity of amyloidogenic peptides by modulating aggregation behaviors. Herein we report an approach toward reducing the neuronal cytotoxicity of amyloidogenic peptides by accelerating the aggregation process, which is different from prevalent methods via inhibiting the aggregation of peptides. The pyridyl derivatives behave like chaperones to dramatically change the assembling characteristics of the peptides via strong hydrogen bond formation with C-termini of amyloid β (Aβ) peptides, which is revealed by using scanning probe microscopy. The light scattering experiments demonstrated the effect of the chaperone-like molecules on accelerating the aggregation process of Aβ peptides, accompanied by the reduced neuronal cytotoxicity of amyloidogenic peptides. These results would give rise to a complementary approach for modulating biological effects of the aggregates of amyloidogenic peptides.

Original languageEnglish (US)
Pages (from-to)6001-6007
Number of pages7
JournalACS Nano
Issue number7
StatePublished - Jul 26 2011
Externally publishedYes


  • amyloidogenic peptide
  • chaperone-like molecules
  • modulation
  • neuronal cytotoxicity
  • peptide aggregation

ASJC Scopus subject areas

  • General Materials Science
  • General Engineering
  • General Physics and Astronomy


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