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氨基酸修饰聚苯乙烯纳米粒子对淀粉样β蛋白纤维形成的双重影响。

Dual effect of amino modified polystyrene nanoparticles on amyloid β protein fibrillation.

机构信息

Centre for BioNano Interactions, School of Chemistry and Chemical Biology, University College Dublin, Belfield, Dublin 4, Ireland.

出版信息

ACS Chem Neurosci. 2010 Apr 21;1(4):279-87. doi: 10.1021/cn900027u. Epub 2010 Jan 27.

Abstract

The fibrillation kinetics of the amyloid β peptide is analyzed in presence of cationic polystyrene nanoparticles of different size. The results highlight the importance of the ratio between the peptide and particle concentration. Depending on the specific ratio, the kinetic effects vary from acceleration of the fibrillation process by reducing the lag phase at low particle surface area in solution to inhibition of the fibrillation process at high particle surface area. The kinetic behavior can be explained if we assume a balance between two different pathways: first fibrillation of free monomer in solution and second nucleation and fibrillation promoted at the particle surface. The overall rate of fibrillation will depend on the interplay between these two pathways, and the predominance of one mechanism over the other will be determined by the relative equilibrium and rate constants.

摘要

不同粒径的阳离子聚苯乙烯纳米颗粒存在时,对淀粉样β肽的纤颤动力学进行了分析。结果突出了肽和颗粒浓度比的重要性。根据特定的比例,动力学效应从在溶液中通过降低低粒子表面积的滞后相来加速纤颤过程,到在高粒子表面积时抑制纤颤过程变化。如果我们假设两种不同途径之间的平衡,那么可以解释这种动力学行为:首先是溶液中游离单体的纤颤,其次是在颗粒表面促进的成核和纤颤。纤颤的总体速率将取决于这两种途径的相互作用,而一种机制相对于另一种机制的优势将取决于相对平衡和速率常数。

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