A Facile Way to Tune Mechanical Properties of Artificial Elastomeric Proteins-Based Hydrogels
A Facile Way to Tune Mechanical Properties of Artificial Elastomeric Proteins-Based Hydrogels
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DOI：
10.1021/la301225w
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发表时间：
2012-05-29
期刊：
影响因子：
3.9
通讯作者：
Li, Hongbin
中科院分区：
文献类型：
--
作者：
Fang, Jie;Li, Hongbin
基于蛋白质的水凝胶因其在生物医学工程和材料科学中的潜在应用而引起了人们的极大兴趣。使用串联模块蛋白(GB1)(8)作为构建块，我们通过光化学交联策略设计了化学交联水凝胶，该策略基于两个相邻的酪氨酸残基交联成双赖氨酸加合物。然而，由于GB1中酪氨酸残基的反应性相对较低，(GB1)(8)基水凝胶的力学性能较差。在这里，我们报告了一种基于Bolton Hunter试剂的简便方法来改善和调整这种基于蛋白质的水凝胶的机械性能。使用Bolton Hunter试剂，我们可以将赖氨酸残基与酚类官能团进行衍生化，从而调节(GB1)(8)的酚类酪氨酸含量。结果表明，随着酚类含量的增加，(GB1)(8)衍生物制备的水凝胶的力学性能有了显著的改善，包括提高了杨氏模量、断裂模数以及降低了溶胀度。这些结果表明，这种衍生化方法在构建具有所需宏观力学性能的蛋白质生物材料方面具有巨大的潜力。
Protein-based hydrogels have attracted considerable interests due to their potential applications in biomedical engineering and material sciences. Using a tandem modular protein (GB1)(8) as building blocks, we have engineered chemically cross-linked hydrogels via a photochemical cross-linking strategy, which is based on the cross-linking of two adjacent tyrosine residues into dityrosine adducts. However, because of the relatively low reactivity of tyrosine residues in GB1, (GB1)(8)-based hydrogels exhibit poor mechanical properties. Here, we report a Bolton Hunter reagent-based, facile method to improve and tune the mechanical properties of such protein-based hydrogels. Using Bolton Hunter reagent, we can derivatize lysine residues with phenolic functional groups to modulate the phenolic (tyrosine-like) content of (GB1)(8). We show that hydrogels made from derivatized (GB1)(8) with increased phenolic content show significantly improved mechanical properties, including improved Young's modulus, breaking modulus as well as reduced swelling. These results demonstrate the great potential of this derivatization method in constructing protein-based biomaterials with desired macroscopic mechanical properties.