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

Journal Article · Fri Jun 23 00:00:00 EDT 2006 · Biochemical and Biophysical Research Communications

DOI:https://doi.org/10.1016/j.bbrc.2006.04.041· OSTI ID:20854304

Klajnert, B ^[1]; Cortijo-Arellano, M ^[2]; Cladera, J ^[2]; Bryszewska, M ^[1]

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1. Department of General Biophysics, University of Lodz (Poland)
2. Department of Biochemistry and Molecular Biology, Universitat Autonoma de Barcelona (Spain)

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 A{beta} 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.

• OSTI ID: 20854304
• Journal Information: Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 1 Vol. 345; ISSN 0006-291X; ISSN BBRCA9
• Country of Publication: United States
• Language: English

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