The assembly of amyloidogenic yeast sup35 as assessed by scanning (atomic) force microscopy: an analogy to linear colloidal aggregation?
The assembly of amyloidogenic yeast sup35 as assessed by scanning (atomic) force microscopy: an analogy to linear colloidal aggregation?
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DOI：
10.1016/s0006-3495(01)75712-8
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发表时间：
2001-07
影响因子：
3.4
通讯作者：
Shaohua Xu;Brooke Bevis;M. Arnsdorf
中科院分区：
文献类型：
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作者：
Shaohua Xu;Brooke Bevis;M. Arnsdorf
淀粉样变性是一类由蛋白质聚集和沉积在各种组织和器官中引起的疾病。本文以酵母淀粉样蛋白形成蛋白Sup35为模型，研究淀粉样纤维的形成。用扫描力显微镜研究了Sup35对淀粉样蛋白形成的动力学。我们发现：1)Sup35纤维的组装始于单个NM肽，这些肽聚集形成大的微球或成核单元，这些微球或成核单元依次形成二聚体、三聚体、四聚体和更长的线性组装，形成一串微球；2)线形组件的形态不同；3)纤维的聚集与胶体粒子的聚集有相似之处。在此基础上提出了一个偶极子装配模型，该模型将允许进一步的实验测试。
Amyloidosis is a class of diseases caused by protein aggregation and deposition in various tissues and organs. In this paper, a yeast amyloid-forming protein Sup35 was used as a model for understanding amyloid fiber formation. The dynamics of amyloid formation by Sup35 were studied with scanning force microscopy. We found that: 1) the assembly of Sup35 fibers begins with individual NM peptides that aggregate to form large beads or nucleation units which, in turn, form dimers, trimers, tetramers and longer linear assemblies appearing as a string of beads; 2) the morphology of the linear assemblies differ; and 3) fiber assembly suggests an analogy to the aggregation of colloidal particles. A dipole assembly model is proposed based on this analogy that will allow further experimental testing.