Catechol‐Amyloid Interactions

• Published in: Chembiochem : a European journal of chemical biology 2023-12, Vol.24 (24), p.e202300628-n/a
• Main Authors: Le, Nghia T. K., Kang, Eun Joo, Park, Ji Hun, Kang, Kyungtae
• Format: Article
• Language: English
• Subjects: amyloid; Amyloid - chemistry; Amyloid beta-Peptides - metabolism; Amyloidogenic Proteins; Biosynthesis; Catechol; Catechols - chemistry; Fibers; Functional groups; Inhibitors; Melanin; Melanins - chemistry; peptide assembly; polyphenolic compounds
• ISSN: 1439-4227; 1439-7633
• DOI: 10.1002/cbic.202300628

This 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. Exploring Interactions: Catechol Molecules and Amyloid Proteins. This review delves into intricate mutual interactions between catechol‐containing molecules and aggregation‐prone proteins. While previous research has primarily focused on unidirectional interactions, we examine their multifaceted dynamics, shedding light on chemical insights and three‐dimensional orientations that may unlock undiscovered roles in supramolecular structures.