Fusion of amyloid beta with ferritin yields an isolated oligomeric beta-sheet-rich aggregate inside the ferritin cage-Reference-Cited by-同舟云学术

Fusion of amyloid beta with ferritin yields an isolated oligomeric beta-sheet-rich aggregate inside the ferritin cage

Published:2024 Issue:9 Volume:12 Page:2408-2417
ISSN:2047-4830
Container-title:Biomaterials Science
language:en
Short-container-title:Biomater. Sci.

Author:

Maity Basudev¹,Kameyama Shiori¹,Tian Jiaxin¹,Pham Thuc Toan¹,Abe Satoshi¹^ORCID,Chatani Eri²,Murata Kazuyoshi³⁴,Ueno Takafumi¹⁵^ORCID

Affiliation:

1. School of Life Science and Technology, Tokyo Institute of Technology, Nagatsuta-cho, 4259, Midori-ku, Yokohama 226 8501, Japan

2. Department of Chemistry, Graduate School of Science, Kobe University, Kobe, Hyogo 657-8501, Japan

3. Exploratory Research Center on Life and Living Systems (ExCELLS), National Institute for Natural Sciences, Okazaki, Aichi, 444-8585, Japan

4. National Institute for Physiological Sciences (NIPS), National Institute for Natural Sciences, Okazaki, Aichi, 444-8585, Japan

5. Living Systems Materialogy (LiSM) Research Group, International Research Frontiers Initiative (IRFI), Tokyo Institute of Technology, Nagatsuta-cho 4259, Midori-ku, Yokohama 226-8501, Japan

Abstract

Amyloid beta peptide is genetically fused with a ferritin monomer. When the 24-mer ferritin cage is formed, 24 Aβ peptides are encapsulated and form a β-sheet-rich oligomer which can be directly visualized by high-speed AFM after cage disassembly.

Funder

Japan Society for the Promotion of Science London

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/BM/D4BM00173G

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