PAMAM dendrimers as potential agents against fibrillation of α-synuclein, a parkinson's disease-related protein.
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Date
2009-03-10
Journal Title
Journal ISSN
Volume Title
Publisher
Wiley-VCH Verlag Berlin
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
Description
Keywords
Small angle scattering, Agglomeration, Peptides, Fluorescence, Amorphous state, Transmission electron microscopy
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. doi:10.1002/mabi.200800242