An amphiphilic material arginine–arginine–bile acid promotes α-synuclein amyloid formation-Reference-Cited by-同舟云学术

An amphiphilic material arginine–arginine–bile acid promotes α-synuclein amyloid formation

Published:2023 Issue:21 Volume:15 Page:9315-9328
ISSN:2040-3364
Container-title:Nanoscale
language:en
Short-container-title:Nanoscale

Author:

Lin Yuxi¹,Park So-Hyeon²³^ORCID,Bok Eugene⁴,Heo Yunseok¹,Yang Seong-Bin³,Yi Yoon-Sun⁵,Lee Jun-Hyuck²³,Seo Donghyun¹⁶,Jo Eunae¹,Lim Sungsu⁷,Kim Yun Kyung⁷⁸^ORCID,Kardos József⁹,Ryu Kyoung-Seok¹¹⁰,Kim Jaekwang⁴,Park Jooho²³,Lee Young-Ho¹¹⁰¹¹^ORCID

Affiliation:

1. Research Center for Bioconvergence Analysis, Korea Basic Science Institute (KBSI), Chungbuk 28119, Republic of Korea

2. Department of Biomedical Chemistry, College of Biomedical & Health Science, Konkuk University, Chungju 27478, Republic of Korea

3. Department of Applied Life Sciences, Graduate School, BK21 Program, Konkuk University, Chungju 27478, Republic of Korea

4. Dementia Research Group, Korea Brain Research Institute (KBRI), Daegu 41062, Republic of Korea

5. Electron Microscopy & Spectroscopy Team, Korea Basic Science Institute (KBSI), Chungbuk 28119, Republic of Korea

6. Department of Proteome Structural Biology, University of Science and Technology (UST), Daejeon 34113, Republic of Korea

7. Brain Science Institute, Korea Institute of Science and Technology (KIST), Seoul 02792, Republic of Korea

8. Division of Bio-Medical Science & Technology, KIST School, University of Science and Technology (UST), Seoul 02792, Republic of Korea

9. Department of Biochemistry, Institute of Biology, ELTE Eötvös Loránd University, H-1117 Budapest, Hungary

10. Bio-Analytical Science, University of Science and Technology (UST), Daejeon 34113, Republic of Korea

11. Graduate School of Analytical Science and Technology (GRAST), Chungnam National University, Daejeon 34134, Republic of Korea

Abstract

We developed a novel amphiphilic material, arginine-arginine (RR)-bile acid (BA). RR-BA selectively binds to aSN in Parkinson’s disease and boosts aSN amyloidogenesis through a mechanism of electrostatic binding-hydrophobic condensation.

Funder

National Research Council of Science and Technology

National Research Foundation of Korea

Ministry of Science and ICT, South Korea

Korea Basic Science Institute

Korea Brain Research Institute

Magyar Tudományos Akadémia

Publisher

Royal Society of Chemistry (RSC)

Subject

General Materials Science

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