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

被引:1
|
作者
van Dalen, Maurice C. E. [1 ,2 ,3 ]
Karperien, Marcel [1 ]
Claessens, Mireille M. A. E. [2 ]
Post, Janine N. [1 ]
机构
[1] Univ Twente, TechMed Ctr, Dev BioEngn, NL-7500 AE Enschede, Overijssel, Netherlands
[2] Univ Twente, Nanobiophys, Mesa, NL-7500 AE Enschede, Netherlands
[3] Scinus Cell Expans Netherlands BV, Bilthoven, Netherlands
来源
ACS OMEGA | 2023年 / 8卷 / 27期
关键词
ALPHA-SYNUCLEIN; FIBRIL FORMATION; CELLULAR DEATH; HYDROGELS; EXPRESSION; COLLAGEN; CHONDROCYTES; REPAIR; BONE; CHONDROGENESIS;
D O I
10.1021/acsomega.3c00151
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
The formation of fibrocartilage during articular cartilageregenerationremains a clinical problem affecting adequate restoration of articularcartilage in joints. To stimulate chondrocytes to form articular cartilage,we investigated the use of amyloid fibril-based scaffolds. The proteins alpha-synuclein, beta-lactoglobulin, and lysozyme were inducedto self-assemble into amyloid fibrils and, during dialysis, formedmicrometer scale amyloid networks that resemble the cartilage extracellularmatrix. Our results show that lysozyme amyloid micronetworks supportedchondrocyte viability and extracellular matrix deposition, while alpha-synucleinand beta-lactoglobulin maintained cell viability. With this study,we not only confirm the possible use of amyloid materials for tissueregeneration but also demonstrate that the choice of protein, ratherthan its amyloid-fold per se, affects the cellular response and tissueformation.
引用
收藏
页码:24198 / 24209
页数:12
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