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PAMAM Dendrimers as Potential Agents against Fibrillation of α ‐Synuclein, a Parkinson's Disease‐Related Protein
Author(s) -
Rekas Agata,
Lo Victor,
Gadd Gerry E.,
Cappai Roberto,
Yun Seok I.
Publication year - 2009
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.200800242
Subject(s) - dendrimer , fibril , fibrillation , biophysics , chemistry , alpha synuclein , inhibitory postsynaptic potential , parkinson's disease , biochemistry , disease , neuroscience , biology , medicine , atrial fibrillation
The effect of PAMAM dendrimers (generations G3, G4 and G5) on the fibrillation of α ‐synuclein was examined by fluorescence and CD spectroscopy, TEM and SANS. PAMAM dendrimers inhibited fibrillation of α ‐synuclein and this effect increased both with generation number and PAMAM concentration. SANS showed structural changes in the formed aggregates of α ‐synuclein – from cylindrical to dense three‐dimensional ones – as the PAMAM concentration increased, on account of the inhibitory effect. PAMAM also effectively promoted the breaking down of pre‐existing fibrils of α ‐synuclein. In both processes – that is, inhibition and disassociation of fibrils – PAMAM redirected α ‐synuclein to an amorphous aggregation pathway.