Structural region essential for amyloid fibril formation in cytochrome <i>c</i> elucidated by optical trapping-Reference-Cited by-同舟云学术

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

Published:2022 Issue:92 Volume:58 Page:12839-12842
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Hirota Shun¹^ORCID,Chiu Chun-Liang²,Chang Chieh-Ju²,Lo Pei-Hua²,Chen Tien²^ORCID,Yang Hongxu¹,Yamanaka Masaru¹,Mashima Tsuyoshi¹^ORCID,Xie Cheng¹^ORCID,Masuhara Hiroshi²^ORCID,Sugiyama Teruki¹²^ORCID

Affiliation:

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

2. Department of Applied Chemistry and Center for Emergent Functional Matter Science, National Yang Ming Chiao Tung University, 1001 University Road, Hsinchu 300093, Taiwan

Abstract

Amyloid fibril formation of cytochrome c is spatially and temporally controlled by the optical trapping method, identifying that the structural change in the region containing Ala83 is essential for the amyloid fibril formation.

Funder

Japan Society for the Promotion of Science

Core Research for Evolutional Science and Technology

Ministry of Education (MOE) in Taiwan

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2022/CC/D2CC04647D

Reference38 articles.

1. Review: History of the Amyloid Fibril

2. Protein Misfolding, Functional Amyloid, and Human Disease

3. Biology of Amyloid: Structure, Function, and Regulation

4. Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer’s Disease, Parkinson’s Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis

5. Biophysical processes underlying cross-seeding in amyloid aggregation and implications in amyloid pathology

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