Modulation effect of filamentous phage on α-synuclein aggregation

Hemi Dimant, Noa Sharon, Beka Solomon

Research output: Contribution to journalArticlepeer-review

Abstract

Conversion of soluble peptides and proteins into amyloid fibrils and/or intermediate oligomers is believed to be the central event in the pathogenesis of most human neurodegenerative diseases, including Parkinson's disease (PD). Here we describe the modulating effect of filamentous phages on aggregation of α-synuclein (AS) in vitro and in a PD cellular model. Filamentous phages, well understood at both structural and genetic levels, have a nanotubular appearance, showing conformational similarities to amyloid fibrils. Since filamentous phages can infect only bacteria and have no tropism to mammalian cells, we utilized the f88 system to present a peptide containing a cyclic RGD (arg-gly-asp), which enabled phage internalization into the cells. Detection of intracellular AS oligomers, in differentiated SH-SY5Y cells, stably transfected with wild type AS gene, was performed using Western blot and ELISA measurements. Data presented here show reduced levels of AS soluble aggregates in phage treated cells compared to non-treated cells, suggesting new therapeutics for PD.

Original languageEnglish
Pages (from-to)491-496
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume383
Issue number4
DOIs
StatePublished - 12 Jun 2009

Keywords

  • Aggregation
  • Amyloid
  • Conformation
  • Filamentous phage
  • Oligomers
  • Parkinson's disease
  • α-Synuclein

Fingerprint

Dive into the research topics of 'Modulation effect of filamentous phage on α-synuclein aggregation'. Together they form a unique fingerprint.

Cite this