Influence of phosphorus dendrimers on the aggregation of the prion peptide PrP 185-208

Barbara Klajnert, Marta Cortijo-Arellano, Josep Cladera, Jean-Pierre Majoral, Anne-Marie Caminade, Maria Bryszewska
Biochemical and Biophysical Research Communications 2007 December 7, 364 (1): 20-5
Inhibition of fibril assembly is a potential therapeutic strategy in prion diseases. The effect of cationic phosphorous dendrimers on the aggregation process of the prion peptide PrP 185-208 was studied using a spectrofluorometric assay with thioflavin T (ThT) and Fourier transformed infrared spectroscopy in order to monitor the kinetics of the process and the changes in the peptide secondary structure. The results show that phosphorous dendrimers are able to clearly interfere with PrP 185-208 aggregation process by both slowing down the formation of aggregates (by causing a decrease of the nucleation rate) and by lowering the final amount of amyloid fibrils, a common hallmark of conformational diseases. The dendrimers effect on the aggregation process would imply their interaction with peptide monomers and oligomers during the nucleation phase.

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