title: Influence of phosphorus dendrimers on the aggregation of the prion peptide PrP 185-208.
abstract: 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.
authors.affiliation: Department of General Biophysics, University of Lodz, 12/16 Banacha Street, 90-237 Lodz, Poland. aklajn@biol.uni.lodz.pl
authors.forename: Barbara
authors.initials: B
authors.lastname: Klajnert
authors.forename: Marta
authors.initials: M
authors.lastname: Cortijo-Arellano
authors.forename: Josep
authors.initials: J
authors.lastname: Cladera
authors.forename: Jean-Pierre
authors.initials: JP
authors.lastname: Majoral
authors.forename: Anne-Marie
authors.initials: AM
authors.lastname: Caminade
authors.forename: Maria
authors.initials: M
authors.lastname: Bryszewska
mesh_terms: D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry / Q000187:drug effects / Q000648:ultrastructure; D052160:Benzothiazoles; D050091:Dendrimers / Q000494:pharmacology*; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry* / Q000648:ultrastructure; D010758:Phosphorus / Q000494:pharmacology*; D018621:PrPC Proteins / Q000737:chemistry* / Q000648:ultrastructure; D011328:Prions / Q000737:chemistry* / Q000187:drug effects / Q000648:ultrastructure; D017433:Protein Structure, Secondary; D013050:Spectrometry, Fluorescence; D017550:Spectroscopy, Fourier Transform Infrared; D013844:Thiazoles
chemical_list: D000682:Amyloid; D052160:Benzothiazoles; D050091:Dendrimers; D010446:Peptide Fragments; D018621:PrPC Proteins; D011328:Prions; D013844:Thiazoles; C524422:prion protein (185-208); C009462:thioflavin T; D010758:Phosphorus