ANSTO Publications Online: PAMAM dendrimers as potential agents against fibrillation of α-synuclein, a parkinson's disease-related protein.

Please use this identifier to cite or link to this item: http://apo.ansto.gov.au/dspace/handle/10238/1851

Title:	PAMAM dendrimers as potential agents against fibrillation of α-synuclein, a parkinson's disease-related protein.
Authors:	Rekas, A Lo, V Gadd, GE Cappai, R Yun, SL
Keywords:	Small Angle Scattering Agglomeration Peptides Fluorescence Amorphous State 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
URI:	http://dx.doi.org/10.1002/mabi.200800242 http://apo.ansto.gov.au/dspace/handle/10238/1851
ISSN:	1616-5187
Appears in Collections:	Journal Articles

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