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Disruption of Amyloid Prion Protein Aggregates by Cationic Pyridylphenylene Dendrimers
Author(s) -
Sorokina Svetlana A.,
Stroylova Yulia Yu.,
Shifrina Zinaida B.,
Muronetz Vladimir I.
Publication year - 2016
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/mabi.201500268
Subject(s) - dendrimer , thioflavin , chemistry , cationic polymerization , protein aggregation , amyloid (mycology) , prion protein , biophysics , fluorescence , inclusion bodies , blot , amyloid fibril , amyloid disease , biochemistry , amyloid β , polymer chemistry , recombinant dna , biology , alzheimer's disease , medicine , inorganic chemistry , physics , disease , pathology , quantum mechanics , gene
Disruption of amyloid protein aggregates is one of the potential therapies for treatment of neurodegenerative disorders such as prion diseases. Here, for the first time we report that pH‐independent cationic pyridylphenylene dendrimers are able to disrupt amyloid protein aggregates at physiological pH as exemplified by inclusion bodies of ovine prion protein. The results show that exposure of inclusion bodies to the dendrimers leads to its partial disaggregation and release of the nanosize protein–dendrimer complexes. The complexes were characterized by SDS PAGE, DLS, and Western blotting methods. Thioflavin T fluorescence clearly demonstrated a decrease of amyloidogenic capability of the prion protein upon exposure to the dendrimers. The complexes formed are stable and do not show further aggregation.