Amyloid fibrils are self-assembled and ordered proteinaceous supramolecules structurally characterized by the cross-β spine. Amyloid formation is known to be related to various diseases typified by neurogenerative disorders and involved in a variety of functional roles. Whereas common mechanisms for amyloid formation have been postulated across diverse systems, the mesoscopic morphology of the fibrils is significantly affected by the type of solution condition in which it grows. Amyloid formation is also thought to share a phenomenological similarity with protein crystallization. Although many studies have demonstrated the effect of gravity on protein crystallization, its effect on amyloid formation has not been reported. In this study, we conducted an experiment at the International Space Station (ISS) to characterize fibril formation of 40-residue amyloid β (Aβ(1–40)) under microgravity conditions. Our comparative analyses revealed that the Aβ(1–40) fibrilization progresses much more slowly on the ISS than on the ground, similarly to protein crystallization. Furthermore, microgravity promoted the formation of distinct morphologies of Aβ(1–40) fibrils. Our findings demonstrate that the ISS provides an ideal experimental environment for detailed investigations of amyloid formation mechanisms by eliminating the conventionally uncontrollable factors derived from gravity.

淀粉样原纤维是自组装且有序的蛋白质性超分子，其结构以交叉-β脊柱为特征。已知淀粉样蛋白的形成与各种以神经发生性疾病为代表的疾病有关，并参与多种功能性作用。尽管已经假设了跨不同系统的淀粉样蛋白形成的常见机制，但是原纤维的介观形态却受到其生长的溶液条件类型的显着影响。淀粉样蛋白的形成也被认为与蛋白质结晶有着相似的现象学相似性。尽管许多研究表明重力对蛋白质结晶的影响，但尚未报道其对淀粉样蛋白形成的影响。在这个研究中，我们在国际空间站（ISS）进行了一项实验，以表征在微重力条件下40残基淀粉样蛋白β（Aβ（1–40））的原纤维形成。我们的比较分析表明，与蛋白质结晶相似，在ISS上Aβ（1–40）的纤维化进程比在地面上要慢得多。此外，微重力促进了Aβ（1–40）原纤维独特形态的形成。我们的发现表明，ISS消除了重力引致的传统不可控因素，为淀粉样蛋白形成机理的详细研究提供了理想的实验环境。类似于蛋白质结晶。此外，微重力促进了Aβ（1–40）原纤维独特形态的形成。我们的发现表明，ISS消除了重力引致的传统不可控因素，为淀粉样蛋白形成机理的详细研究提供了理想的实验环境。类似于蛋白质结晶。此外，微重力促进了Aβ（1–40）原纤维独特形态的形成。我们的发现表明，ISS消除了重力引致的传统不可控因素，为淀粉样蛋白形成机理的详细研究提供了理想的实验环境。