Characterization of conformational dynamics of the active end of amyloid fibril to elucidate mechanisms underlying the fibril elongation

为了表征淀粉样纤维活性末端的构象动力学，我们尝试设计小尺寸的淀粉样纤维模型。我们成功地制备了淀粉样β（Aβ）分子的串联重复序列作为淀粉样纤维的最小模型。结果表明，Aβ串联重复序列可被Aβ淀粉样纤维末端特异性抗体识别，并作为核心促进淀粉样纤维化。此外，我们发现细菌分子伴侣和神经节苷脂包埋的双胞体可以抑制Aβ纤维的形成。

To characterize the conformational dynamics of the active end of amyloid fibril, we attempted to design small-sized amyloid fibril models. We successfully prepared tandem repeats of amyloid β (Aβ) molecules as minimal models of the amyloid fibrils by genetic manipulation. It was revealed that the tandem-repeat Aβ was recognized by the specific antibody directed against the end point of Aβ amyloid fibrils and served as nucleus which promoted the amyloid fibrillization. Furthermore, we found that bacterial molecular chaperones and ganglioside-embedding bicelles could suppress formation of Aβ fibrils.