Utilizing Frémy's Salt to Increase the Mechanical Rigidity of Supramolecular Peptide-Based Gel Networks.
Utilizing Frémy's Salt to Increase the Mechanical Rigidity of Supramolecular Peptide-Based Gel Networks.
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DOI：
10.3389/fbioe.2020.594258
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发表时间：
2020
影响因子：
5.7
通讯作者：
Schneider JP
中科院分区：
文献类型：
--
作者：
Fichman G;Schneider JP
肽基超分子凝胶是一类重要的生物材料，可用于从药物递送到组织工程的生物医学应用。允许人们容易地调节这些凝胶的机械性质的方法将允许甚至更广泛的应用。Frémy盐是一种无机盐和长寿命的自由基，已知其可氧化酚类。在本文中，我们表明Frémy盐可用于显著增加由含酪氨酸的自组装β-发夹肽形成的水凝胶的机械刚度。当将Frémy盐加入到预先形成的凝胶中时，它将酪氨酸残基转化为邻醌，邻醌随后可以与组装肽的赖氨酸侧链中存在的胺反应。这导致化学交联的安装，加强凝胶基质。我们使用紫外-可见光谱，透射电子显微镜和流变学测量，其特征在于未氧化和氧化的凝胶系统，并表明Frémy盐增加了凝胶刚性近一个数量级，同时保持凝胶的剪切稀/恢复行为。因此，Frémy盐代表了调节基于肽的自组装凝胶的机械刚性的按需方法。
Peptide-based supramolecular gels are an important class of biomaterials that can be used for biomedical applications ranging from drug delivery to tissue engineering. Methodology that allows one to readily modulate the mechanical properties of these gels will allow yet even a broader range of applications. Frémy's salt is an inorganic salt and long-lived free radical that is known to oxidize phenols. Herein, we show that Frémy's salt can be used to dramatically increase the mechanical rigidity of hydrogels formed by tyrosine-containing self-assembling β-hairpin peptides. When Frémy's salt is added to pre-formed gels, it converts tyrosine residues to o-quinones that can subsequently react with amines present within the lysine side chains of the assembled peptide. This results in the installation of chemical crosslinks that reinforce the gel matrix. We characterized the unoxidized and oxidized gel systems using UV-Vis, transmission electron microscopy and rheological measurements and show that Frémy's salt increases the gel rigidity by nearly one order of magnitude, while retaining the gel's shear-thin/recovery behavior. Thus, Frémy's salt represents an on-demand method to modulate the mechanical rigidity of peptide-based self-assembled gels.