Influence of dendrimer's structure on its activity against amyloid fibril formation

B. Klajnert, M. Cortijo-Arellano, J. Cladera, M. Bryszewska

Research output: Contribution to journalArticleResearchpeer-review

123 Citations (Scopus)

Abstract

Inhibition of fibril assembly is a potential therapeutic strategy in neurodegenerative disorders such as prion and Alzheimer's diseases. Highly branched, globular polymers-dendrimers-are novel promising inhibitors of fibril formation. In this study, the effect of polyamidoamine (PAMAM) dendrimers (generations 3rd, 4th, and 5th) on amyloid aggregation of the prion peptide PrP 185-208 and the Alzheimer's peptide Aβ 1-28 was examined. Amyloid fibrils were produced in vitro and their formation was monitored using the dye thioflavin T (ThT). Fluorescence studies were complemented with electron microscopy. The results show that the higher the dendrimer generation, the larger the degree of inhibition of the amyloid aggregation process and the more effective are dendrimers in disrupting the already existing fibrils. A hypothesis on dendrimer-peptide interaction mechanism is presented based on the dendrimers' molecular structure. © 2006 Elsevier Inc. All rights reserved.
Original languageEnglish
Pages (from-to)21-28
JournalBiochemical and Biophysical Research Communications
Volume345
Issue number1
DOIs
Publication statusPublished - 23 Jun 2006

Keywords

  • Aggregation
  • Alzheimer
  • Amyloid peptide
  • Dendrimer
  • Prion

Fingerprint

Dive into the research topics of 'Influence of dendrimer's structure on its activity against amyloid fibril formation'. Together they form a unique fingerprint.

Cite this