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|Title: ||PAMAM dendrimers as potential agents against fibrillation of α-synuclein, a parkinson's disease-related protein.|
|Authors: ||Rekas, A|
|Keywords: ||Small Angle Scattering|
Transmission Electron Microscopy
|Issue Date: ||10-Mar-2009|
|Publisher: ||Wiley-VCH Verlag Berlin|
|Citation: ||Rekas, A., Lo, V., Gadd, G. E., Cappai, R., & Yun, S. L. (2009). PAMAM dendrimers as potential agents against fibrillation of α-synuclein, a parkinson's disease-related protein. Macromolecular Bioscience, 9(3), 230-238.|
|Abstract: ||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. © 2009, Wiley-VCH Verlag Berlin|
|Appears in Collections:||Journal Articles|
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