Catechol‐Amyloid Interactions

Author:

Le Nghia T. K.1,Kang Eun Joo1,Park Ji Hun2,Kang Kyungtae1ORCID

Affiliation:

1. Department of Applied Chemistry Kyung Hee University Yongin, Gyeonggi 17104 South Korea

2. Department of Science Education Ewha Womans University Seoul 03760 South Korea

Abstract

AbstractThis review introduces multifaceted mutual interactions between molecules containing a catechol moiety and aggregation‐prone proteins. The complex relationships between these two molecular species have previously been elucidated primarily in a unidirectional manner, as demonstrated in cases involving the development of catechol‐based inhibitors for amyloid aggregation and the elucidation of the role of functional amyloid fibers in melanin biosynthesis. This review aims to consolidate scattered clues pertaining to catechol‐based amyloid inhibitors, functional amyloid scaffold of melanin biosynthesis, and chemically designed peptide fibers for providing chemical insights into the role of the local three‐dimensional orientation of functional groups in manifesting such interactions. These orientations may play crucial, yet undiscovered, roles in various supramolecular structures.

Funder

National Research Foundation of Korea

Ministry of Science and ICT, South Korea

Publisher

Wiley

Subject

Organic Chemistry,Molecular Biology,Molecular Medicine,Biochemistry

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