Photopolymerized thermosensitive hydrogels for tailorable diffusion-controlled protein delivery
Photopolymerized thermosensitive hydrogels for tailorable diffusion-controlled protein delivery
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DOI：
10.1016/j.jconrel.2009.06.003
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发表时间：
2009-12-16
影响因子：
10.8
通讯作者：
Hennink, W. E.
中科院分区：
文献类型：
--
作者：
Censi, R.;Vermonden, T.;Hennink, W. E.
在本文中，研究了定制光聚合热敏水凝胶的降解和蛋白质释放行为的可能性。该水凝胶由ABA三嵌段共聚物组成，其中热敏A嵌段是甲基丙烯酸酯化聚(N-(2-羟丙基)甲基丙烯酰胺乳酸酯)，B嵌段是分子量为10 kDa的聚乙二醇。这些水凝胶是通过物理和化学交联方法的结合来制备的。当热敏甲基丙烯酸酯 p(HPMAm-lac)-PEG-p(HPMAm-lac) 的溶液被加热至其浊点以上时，获得粘弹性材料，该材料可以通过光聚合引入共价交联来稳定。通过改变聚合物浓度，形成具有不同机械性能的水凝胶，其交联密度、网格尺寸、溶胀和降解行为可以调节。结果表明，三种模型蛋白（溶菌酶、BSA 和 IgG，流体动力学直径范围为 4.1 至 10.7 nm）的释放速率取决于交联之间的蛋白大小和水凝胶分子量，并受 Fickian 扩散控制。重要的是，封装的蛋白质被定量释放，并且溶菌酶的二级结构和酶活性被完全保留，证明了所研究的递送系统的蛋白质友好性质。 (C) 2009 Elsevier B.V. 保留所有权利。
In this paper the possibility to tailor degradation and protein release behavior of photo polymerized thermosensitive hydrogels is studied. The hydrogels consist of ABA triblock copolymer, in which the thermosensitive A-blocks are methacrylated poly(N-(2-hydroxypropyl)methacrylamide lactate)s and the B-block is poly(ethylene glycol) with molecular weight of 10 kDa. These hydrogels are prepared by using a combination of physical and chemical cross-linking methods. When a solution of a thermosensitive methacrylated p(HPMAm-lac)-PEG-p(HPMAm-lac) is heated above its cloud point a viscoelastic material is obtained, which can be stabilized by introducing covalent cross-links by photopolymerization. By varying the polymer concentration, hydrogels with different mechanical properties are formed, of which the cross-linking density, mesh size, swelling and degradation behavior can be tuned. It was demonstrated that the release rate of three model proteins (lysozyme, BSA and IgG, with hydrodynamic diameters ranging from 4.1 to 10.7 nm) depended on the protein size and hydrogel molecular weight between cross-links and was governed by the Fickian diffusion. Importantly, the encapsulated proteins were quantitatively released and the secondary structure and the enzymatic activity of lysozyme were fully preserved demonstrating the protein friendly nature of the studied delivery system. (C) 2009 Elsevier B.V. All rights reserved.