Directional BMP-2 for functionalization of titanium surfaces
Directional BMP-2 for functionalization of titanium surfaces
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DOI：
10.1016/j.biomaterials.2008.10.040
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发表时间：
2009-02-01
期刊：
影响因子：
14
通讯作者：
Shiba, Kiyotaka
中科院分区：
文献类型：
--
作者：
Kashiwagi, Kenji;Tsuji, Toru;Shiba, Kiyotaka
生物大分子在材料表面的高效固定化是再生医学和组织工程领域发展的关键。然而，细胞因子在表面的强烈和不可逆转的固定往往会削弱它们的生物学功能。材料表面和生物分子之间的破坏性疏水相互作用可能是这种失活的基础。或者，细胞因子与物质的解离可能是信号转导所必需的。在这里，我们提出了一种将细胞因子固定在材料表面的新方法：使用材料结合的人工肽来介导细胞因子与材料表面之间的可逆相互作用。我们创造了含有三个钛结合基序的人造蛋白，并将它们融合到BMP-2的N端。重组BMP-2可与钛表面可逆结合，并诱导BMP信号转导活性。当缺乏钛结合基序的疏水蛋白与BMP-2融合时，该蛋白与钛表面紧密结合，但几乎没有BMP活性，证实了固定化方式的重要性。(C)2008爱思唯尔有限公司。保留所有权利。
Efficient immobilization of biomacromolecules on material surfaces is a key to development in areas of regenerative medicine and tissue engineering. However, strong and irreversible immobilization of cytokines on surfaces often diminishes their biological functionality. A destructive hydrophobic interaction between the material surface and the biomolecule may underlie this inactivation. Alternatively, dissociation of the cytokine from the material may be necessary for signal transduction. Here we propose a new method for immobilizing cytokines on material surfaces: a material-binding artificial peptide is used to mediate reversible interaction between the cytokine and the material surface. We created artificial proteins that contained three copies of a Ti-binding motif, and fused them to the N-terminal of BMP-2. The engineered BMP-2 showed reversible binding to Ti surfaces and induced BMP signaling activity. When a hydrophobic protein devoid of the Ti-binding motif was fused to BMP-2, the protein tightly bound to Ti surfaces but showed little BMP activity, confirming the importance of the mode of immobilization. (C) 2008 Elsevier Ltd. All rights reserved.