Small stress molecules inhibit aggregation and neurotoxicity of prion peptide 106-126

Mathumai Kanapathipillai, Sook Hee Ku, Koyeli Girigoswami, Chan Beum Park

Research output: Contribution to journalArticlepeer-review

36 Scopus citations

Abstract

In prion diseases, the posttranslational modification of host-encoded prion protein PrPc yields a high β-sheet content modified protein PrPsc, which further polymerizes into amyloid fibrils. PrP106-126 initiates the conformational changes leading to the conversion of PrPc to PrPsc. Molecules that can defunctionalize such peptides can serve as a potential tool in combating prion diseases. In microorganisms during stressed conditions, small stress molecules (SSMs) are formed to prevent protein denaturation and maintain protein stability and function. The effect of such SSMs on PrP106-126 amyloid formation is explored in the present study using turbidity, atomic force microscopy (AFM), and cellular toxicity assay. Turbidity and AFM studies clearly depict that the SSMs-ectoine and mannosylglyceramide (MGA) inhibit the PrP106-126 aggregation. Our study also connotes that ectoine and MGA offer strong resistance to prion peptide-induced toxicity in human neuroblastoma cells, concluding that such molecules can be potential inhibitors of prion aggregation and toxicity.

Original languageEnglish (US)
Pages (from-to)808-813
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume365
Issue number4
DOIs
StatePublished - Jan 25 2008

Keywords

  • Cytotoxicity
  • Ectoine
  • Mannosylglyceramide
  • Prion
  • Small stress molecules

Fingerprint

Dive into the research topics of 'Small stress molecules inhibit aggregation and neurotoxicity of prion peptide 106-126'. Together they form a unique fingerprint.

Cite this