Harper J D, Wong S S, Lieber C M, Lansbury P T
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Chem Biol. 1997 Feb;4(2):119-25. doi: 10.1016/s1074-5521(97)90255-6.
Brain amyloid plaque, a diagnostic feature of Alzheimer's disease (AD), contains an insoluble fibrillar core that is composed primarily of variants of the beta-amyloid protein (Abeta). As Abeta amyloid fibrils may initiate neurodegeneration, the inhibition of fibril formation is a possible therapeutic strategy. Very little is known about the early steps of the process, however.
Atomic force microscopy was used to follow amyloid fibril formation in vitro by the Abeta variants Abeta1-40 and Abeta1-42. Both variants first form small ordered aggregates that grow slowly and then rapidly disappear, while prototypical amyloid fibrils of two discrete morphologies appear. Abeta1-42 aggregates much more rapidly than Abeta1-40, which is consistent with its connection to early-onset AD. We propose that the metastable intermediate species be called Abeta amyloid protofibrils.
Abeta protofibrils are likely to be intermediates in the in vitro assembly of Abeta amyloid fibrils, but their in vivo role has yet to be determined. Numerous reports of a nonfibrillar form of Abeta aggregate in the brains of individuals who are predisposed to AD suggest the existence of a precursor form, possibly the protofibril. Thus, stabilization of Abeta protofibrils may be a useful therapeutic strategy.
脑淀粉样斑块是阿尔茨海默病(AD)的一个诊断特征,其包含一个主要由β-淀粉样蛋白(Aβ)变体组成的不溶性纤维状核心。由于Aβ淀粉样纤维可能引发神经退行性变,抑制纤维形成是一种可能的治疗策略。然而,对于该过程的早期步骤知之甚少。
利用原子力显微镜在体外追踪Aβ变体Aβ1-40和Aβ1-42形成淀粉样纤维的过程。两种变体均首先形成小的有序聚集体,这些聚集体生长缓慢,然后迅速消失,同时出现两种不同形态的典型淀粉样纤维。Aβ1-42聚集体的速度比Aβ1-40快得多,这与其与早发性AD的关联一致。我们建议将这种亚稳态中间物种称为Aβ淀粉样前原纤维。
Aβ前原纤维可能是Aβ淀粉样纤维体外组装过程中的中间体,但其在体内的作用尚未确定。众多关于易患AD个体大脑中存在非纤维状Aβ聚集体形式的报道表明存在一种前体形式,可能就是前原纤维。因此,稳定Aβ前原纤维可能是一种有用的治疗策略。