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

Chem Commun (Camb). 2022 Nov 17;58(92):12839-12842. doi: 10.1039/d2cc04647d.

Authors

Affiliations

¹ Division of Materials Science, Graduate School of Science and Technology, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan. [email protected].
² Department of Applied Chemistry and Center for Emergent Functional Matter Science, National Yang Ming Chiao Tung University, 1001 University Road, Hsinchu 300093, Taiwan. [email protected].

PMID: 36315406
DOI: 10.1039/d2cc04647d

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.

MeSH terms

Amyloid* / chemistry
Cysteine / chemistry
Cytochromes c*
Optical Tweezers

Substances

Amyloid
Cytochromes c
Cysteine