PAMAM Dendrimers as Potential Agents against Fibrillation of α-Synuclein, a Parkinson's Disease-Related Protein

被引：58
|
作者：
Rekas, Agata [1 ]
Lo, Victor [1 ]
Gadd, Gerry E. [1 ]
Cappai, Roberto [2 ]
Yun, Seok I. [1 ]
机构：
[1] Australian Nucl Sci & Technol Org, Menai, NSW 2234, Australia
[2] Univ Melbourne, Dept Pathol, Melbourne, Vic 3010, Australia
来源：
MACROMOLECULAR BIOSCIENCE | 2009年 / 9卷 / 03期
关键词：
alpha-synuclein; amorphous; amyloid; dendrimers; neutron scattering; ANGLE NEUTRON-SCATTERING; ALZHEIMERS-DISEASE; AMYLOID PEPTIDES; MOLECULAR CHAPERONE; AGGREGATION; DEPENDENCE; INCLUSIONS; CRYSTALLIN; COMPONENT; NACP;
D O I：
10.1002/mabi.200800242
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The effect of PAMAM dendrimers (generations G3, G4 and G5) on the fibrillation of a-synuclein was examined by fluorescence and CD spectroscopy, TEM and SANS. PAMAM dendrimers inhibited fibrillation of a-synuclein and this effect increased both with generation number and PAMAM concentration. SANS showed structural changes in the formed aggregates of alpha-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 alpha-synuclein. In both processes-that is, inhibition and disassociation of fibrils-PAMAM redirected alpha-synuclein to an amorphous aggregation pathway.
引用
收藏
页码：230 / 238
页数：9
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