Structural region essential for amyloid fibril formation in cytochrome c elucidated by optical trapping

Shun Hirota; Chun-Liang Chiu; Chieh-Ju Chang; Pei-Hua Lo; Tien Chen; Hongxu Yang; Masaru Yamanaka; Tsuyoshi Mashima; Cheng Xie; Hiroshi Masuhara; Teruki Sugiyama

doi:10.1039/D2CC04647D

Structural region essential for amyloid fibril formation in cytochrome c elucidated by optical trapping†

Shun Hirota,

*^a Chun-Liang Chiu,^b Chieh-Ju Chang,^b Pei-Hua Lo,^b Tien Chen,

^b Hongxu Yang,^a Masaru Yamanaka,^a Tsuyoshi Mashima,

^a Cheng Xie,

^a Hiroshi Masuhara

^b and Teruki Sugiyama

*^ab

Author affiliations

* Corresponding authors

^a Division of Materials Science, Graduate School of Science and Technology, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan
E-mail: hirota@ms.naist.jp

^b Department of Applied Chemistry and Center for Emergent Functional Matter Science, National Yang Ming Chiao Tung University, 1001 University Road, Hsinchu 300093, Taiwan
E-mail: sugiyama@nycu.edu.tw

Abstract

Amyloid fibril formation of cytochrome c is spatially and temporally controlled with a combined method of disulfide bond cross-linking of cysteine-introduced variants and optical trapping, identifying that the structural change in the region containing Ala83 is essential for the amyloid fibril formation.

Chemical Communications

Structural region essential for amyloid fibril formation in cytochrome c elucidated by optical trapping†

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Structural region essential for amyloid fibril formation in cytochrome c elucidated by optical trapping

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