open access

https://hdl.handle.net/2115/70685

A Single Spherical Assembly of Protein Amyloid Fibrils Formed by Laser Trapping

英語

spatio-temporal formation

2017-06-06

Wiley-Blackwell

Angewandte chemie-international edition

56(24)

6739-6743

Protein amyloids have received much attention owing to their correlation with serious diseases and to their promising mechanical and optical properties as future materials. Amyloid formation has been conducted by tuning temperature and chemical conditions, so that its nucleation and the following growth are analyzed as ensemble dynamics. A single spherical assembly of amyloid fibrils of cytochrome c domain-swapped dimer was successfully generated upon laser trapping. The amyloid fibrillar structure was confirmed by fluorescence characterization and electron microscopy. The prepared spheres were further manipulated individually in solution to fabricate a three-dimensional microstructure and a line pattern. Amyloid formation dynamics and amyloid-based microstructure fabrication are demonstrated based on direct observation of a single spherical assembly, which foresees a new approach in amyloid studies.

学術雑誌論文

Accepted Manuscript

This is the peer reviewed version of the following article: K. Yuyama, M. Ueda, S. Nagao, S. Hirota, T. Sugiyama, H. Masuhara, Angew. Chem. Int. Ed. 2017, 56, 6739, which has been published in final form at http://dx.doi.org/10.1002/anie.201702352. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.

1433-7851