Fabricating spatially functionalized 3D-printed scaffolds for osteochondral tissue engineering.
Fabricating spatially functionalized 3D-printed scaffolds for osteochondral tissue engineering.
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DOI：
10.14440/jbm.2021.353
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发表时间：
2021
期刊：
影响因子：
--
通讯作者：
Chow LW
中科院分区：
文献类型：
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作者：
Camacho P;Fainor M;Seims KB;Tolbert JW;Chow LW
生物可降解聚合物的三维（3D）打印已迅速成为创建组织工程支架的流行方法。这种技术能够制造复杂的架构，并以高分辨率逐层空间控制多个组件。由此产生的支架还可以在表面上呈现不同的化学基团或生物活性线索，以指导细胞行为。然而，表面功能化通常包括一个或多个制造后处理步骤，其通常产生具有均匀分布的化学物质的生物材料，所述化学物质不能模拟天然组织中发现的生物化学组织。作为替代方案，我们的实验室开发了一种新的方法，将溶剂浇铸3D打印与肽-聚合物缀合物相结合，在单个支架中空间呈现多种生化线索，而不需要制造后的修改。在这里，我们描述了一个详细的，逐步的协议，制造肽功能化的支架和表征其物理结构和生化空间组织。我们使用这些3D打印支架通过控制软骨促进和骨促进肽的空间呈现来指导人间充质干细胞分化和骨软骨组织形成。该方案还描述了如何接种支架和评估由肽组织驱动的基质沉积。
Three-dimensional (3D) printing of biodegradable polymers has rapidly become a popular approach to create scaffolds for tissue engineering. This technique enables fabrication of complex architectures and layer-by-layer spatial control of multiple components with high resolution. The resulting scaffolds can also present distinct chemical groups or bioactive cues on the surface to guide cell behavior. However, surface functionalization often includes one or more post-fabrication processing steps, which typically produce biomaterials with homogeneously distributed chemistries that fail to mimic the biochemical organization found in native tissues. As an alternative, our laboratory developed a novel method that combines solvent-cast 3D printing with peptide-polymer conjugates to spatially present multiple biochemical cues in a single scaffold without requiring post-fabrication modification. Here, we describe a detailed, stepwise protocol to fabricate peptide-functionalized scaffolds and characterize their physical architecture and biochemical spatial organization. We used these 3D-printed scaffolds to direct human mesenchymal stem cell differentiation and osteochondral tissue formation by controlling the spatial presentation of cartilage-promoting and bone-promoting peptides. This protocol also describes how to seed scaffolds and evaluate matrix deposition driven by peptide organization.