Choice of Protein, Not Its Amyloid-Fold, Determines the Success of Amyloid-Based Scaffolds for Cartilage Tissue Regeneration

Maurice C.E. van Dalen, Marcel Karperien, Mireille M.A.E. Claessens, Janine N. Post*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

2 Citations (Scopus)
79 Downloads (Pure)

Abstract

The formation of fibrocartilage during articular cartilage regeneration remains a clinical problem affecting adequate restoration of articular cartilage in joints. To stimulate chondrocytes to form articular cartilage, we investigated the use of amyloid fibril-based scaffolds. The proteins α-synuclein, β-lactoglobulin, and lysozyme were induced to self-assemble into amyloid fibrils and, during dialysis, formed micrometer scale amyloid networks that resemble the cartilage extracellular matrix. Our results show that lysozyme amyloid micronetworks supported chondrocyte viability and extracellular matrix deposition, while α-synuclein and β-lactoglobulin maintained cell viability. With this study, we not only confirm the possible use of amyloid materials for tissue regeneration but also demonstrate that the choice of protein, rather than its amyloid-fold per se, affects the cellular response and tissue formation.
Original languageEnglish
Pages (from-to)24198-24209
Number of pages12
JournalACS Omega
Volume8
Issue number27
Early online date14 Jun 2023
DOIs
Publication statusPublished - 11 Jul 2023

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