Molecular interactions of dendrimers with amyloid peptides: pH dependence

Barbara Klajnert, J. Cladera, M. Bryszewska

Research output: Contribution to journalArticleResearchpeer-review

65 Citations (Scopus)

Abstract

The formation of amyloid plaques is a key pathological event in neurodegenerative disorders, such as prion and Alzheimer's diseases. Dendrimers are considered promising therapeutic agents in these disorders. In the present work, we have studied the effect of polypropyleneimine dendrimers on the formation of amyloid fibrils as a function of pH in order to gain further insight in the aggregation mechanism and its inhibition. Amyloid fibrils from prion peptide PrP 185-208 and Alzheimer's peptide Aβ 1-28 were produced in vitro, and their formation was monitored using the dye thioflavin T (ThT). The results showed that the level of protonation of His, Glu, and Asp residues is important for the final effect, especially at low dendrimer concentration when their inhibiting capacity depends on the pH. At the highest concentrations, dendrimers were very effective against fibril formations for both prion and Alzheimer's peptides. © 2006 American Chemical Society.
Original languageEnglish
Pages (from-to)2186-2191
JournalBiomacromolecules
Volume7
Issue number7
DOIs
Publication statusPublished - 1 Jul 2006

Fingerprint

Dive into the research topics of 'Molecular interactions of dendrimers with amyloid peptides: pH dependence'. Together they form a unique fingerprint.

Cite this