Catechol-Amyloid Interactions

Nghia T.K. Le, Eun Joo Kang, Ji Hun Park, Kyungtae Kang

Research output: Contribution to journalReview articlepeer-review

Abstract

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.

Original languageEnglish
Article numbere202300628
JournalChemBioChem
Volume24
Issue number24
DOIs
StatePublished - 14 Dec 2023

Bibliographical note

Publisher Copyright:
© 2023 Wiley-VCH GmbH.

Keywords

  • amyloid
  • catechol
  • melanin
  • peptide assembly
  • polyphenolic compounds

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