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N-终端扩展阻碍了Aβ42纤维素的形成,但允许与Aβ42进行交叉播种和凝聚

Olga Szczepankiewicz¹, Björn Linse¹, Georg Meisl²

¹Department of Biochemistry and Structural Biology, Lund University , P O Box 124, 221 00 Lund, Sweden.

Journal of the American Chemical Society

|November 5, 2015

概括

新发现的N-终端扩展的粉样β蛋白 (NTE-Aβ) 变体的聚合速度较慢,但仍然可以聚合和交叉种子,可能影响阿尔茨海默病的进展.

科学领域:

神经科学
生物化学
物理化学

背景情况:

粉样β蛋白 (Aβ) 聚合是阿尔茨海默氏症发病的关键.
自然存在的Aβ变体,包括N-终端扩展形式 (NTE-Aβ),存在于体内.
对于NTE-Aβ对聚合动力学和纤维细胞形成的影响尚不完全理解.

研究的目的:

研究具有N端延伸的Aβ42变体的聚合动态和纤维状形态.
阐明影响NTE-Aβ变体聚合率的基本机制.
探索NTE-Aβ和标准Aβ42之间的协聚和交叉催化潜力.

主要方法:

提奥夫拉T光测定用于监测聚合动力学.
传输电子显微镜 (TEM) 来分析纤维状形态.
蒙特卡洛模拟模拟聚动态.
全球运动分析以确定微观速率常数.

主要成果:

NTE-Aβ变体形成与Aβ42相似的粉状纤维.
聚合半衰期 (t1/2) 随着N终端延伸长度的增加而呈指数增长.
对于NTE-Aβ变体,核和延长的微观速率常数被减少.
在Aβ42和NTE-Aβ42之间发生凝聚和交叉催化,尽管NTE-Aβ单体的播种率降低.

结论:

通过物理化学效应,N端延伸显著减缓了Aβ42聚合动力学.
尽管动力较慢,NTE-Aβ变体可以形成混合纤维,并通过凝聚和交叉播种影响聚合.
这些发现突显了NTE-Aβ在体内阿尔茨海默病病理学的潜在作用.

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