Premium
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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom