Chemical and mechanistic analysis of photodynamic inhibition of Alzheimer's β-amyloid aggregation-Reference-Cited by-同舟云学术

Chemical and mechanistic analysis of photodynamic inhibition of Alzheimer's β-amyloid aggregation

Published:2019 Issue:8 Volume:55 Page:1152-1155
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Ahn Minkoo¹²³⁴⁵^ORCID,Lee Byung Il⁶⁷⁸⁹¹⁰,Chia Sean¹²³⁴⁵,Habchi Johnny¹²³⁴⁵,Kumita Janet R.¹²³⁴⁵,Vendruscolo Michele¹²³⁴⁵^ORCID,Dobson Christopher M.¹²³⁴⁵,Park Chan Beum⁶⁷⁸⁹¹⁰^ORCID

Affiliation:

1. Centre for Misfolding Diseases

2. Department of Chemistry

3. University of Cambridge

4. Cambridge

5. UK

6. KAIST Institute for the BioCentury

7. Department of Materials Science and Engineering

8. Korea Advanced Institute of Science and Technology (KAIST)

9. Daejeon 34141

10. Republic of Korea

Abstract

Inhibition of Aβ₄₂ aggregation by photoexcited thioflavin T that generates singlet oxygen to oxidize monomeric Aβ₄₂.

Funder

National Research Foundation of Korea

Agency for Science, Technology and Research

Wellcome Trust

University of Cambridge

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/2019/CC/C8CC09288E

Reference24 articles.

1. Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade

2. Binding Modes of Thioflavin-T to the Single-Layer β-Sheet of the Peptide Self-Assembly Mimics

3. Molecular Rotors: What Lies Behind the High Sensitivity of the Thioflavin-T Fluorescent Marker

4. Ultrafast Bond Twisting Dynamics in Amyloid Fibril Sensor

5. An Analytical Solution to the Kinetics of Breakable Filament Assembly

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