聚酰胺-胺（PAMAM）树枝状大分子作为抗α-突触核蛋白（一种与帕金森病相关的蛋白质）纤维化的潜在药物。
PAMAM dendrimers as potential agents against fibrillation of alpha-synuclein, a Parkinson's disease-related protein.
作者信息
Rekas Agata, Lo Victor, Gadd Gerry E, Cappai Roberto, Yun Seok I
机构信息
Australian Nuclear Science and Technology Organization, PMB 1, Menai, NSW 2234, Australia.
出版信息
Macromol Biosci. 2009 Mar 10;9(3):230-8. doi: 10.1002/mabi.200800242.
The effect of PAMAM dendrimers (generations G3, G4 and G5) on the fibrillation of alpha-synuclein was examined by fluorescence and CD spectroscopy, TEM and SANS. PAMAM dendrimers inhibited fibrillation of alpha-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.
通过荧光光谱、圆二色光谱、透射电子显微镜（TEM）和小角中子散射（SANS）研究了聚酰胺-胺型（PAMAM）树枝状大分子（G3、G4和G5代）对α-突触核蛋白纤维化的影响。PAMAM树枝状大分子抑制α-突触核蛋白的纤维化，且这种作用随代数和PAMAM浓度的增加而增强。小角中子散射显示，由于其抑制作用，随着PAMAM浓度的增加，α-突触核蛋白形成的聚集体结构发生变化，从圆柱形变为致密的三维结构。PAMAM还能有效促进已存在的α-突触核蛋白纤维的分解。在这两个过程中，即纤维的抑制和解离过程中，PAMAM使α-突触核蛋白转向无定形聚集途径。
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