Crosslinking of collagen gels by transglutaminase
Crosslinking of collagen gels by transglutaminase
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DOI：
10.1002/jbm.a.20110
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发表时间：
2004-03-15
影响因子：
4.9
通讯作者：
Vorp, DA
中科院分区：
文献类型：
--
作者：
Orban, JM;Wilson, LB;Vorp, DA
胶原蛋白通常用作组织工程支架，但其在体内的应用受到机械强度不足的限制。本工作的目的是探索利用一种独特的酶交联程序，旨在改善胶原基支架材料的机械性能。I型牛胶原蛋白凝胶通过转氨酶交联，所述转氨酶选择性地介导相邻蛋白质纤维上的谷氨酰胺和赖氨酸残基之间的化学反应，从而提供用于增强三维基质的共价酰胺键。通过热分析和胺基含量验证了交联度。交联胶原的变性温度最高可达66 ± 1 ℃。证实该化学反应对从新西兰白色兔获得的骨髓基质细胞无细胞毒性。发现由交联胶原和骨髓基质细胞形成的管状细胞构建体具有显著高于其非交联类似物的破裂压力（71 +/-4 mmHg vs. 46 +/-3 mmHg; p < 0.01）。因此，转氨酶介导的反应用于成功地强化胶原蛋白凝胶，同时保持对细胞的良性。(C)2004 Wiley Periodicals，Inc.
Collagen is commonly used as a tissue-engineering scaffold, yet its in vivo applications are limited by a deficiency in mechanical strength. The purpose of this work was to explore the utilization of a unique enzymatic crosslinking procedure aimed at improving the mechanical properties of collagen-based scaffold materials. Type I bovine collagen gel was crosslinked by transglutaminase, which selectively mediates the chemical reaction between glutamine and lysine residues on adjacent protein fibers, thus providing covalent amide bonds that serve to reinforce the three-dimensional matrix. The degree of crosslinking was verified by thermal analysis and amine group content. The denaturation temperature of crosslinked collagen reached a maximum of 66 +/- 1degreesC. The chemical reaction was confirmed to be noncytotoxic with respect to bone marrow stromal cells acquired from New Zealand White rabbits. Tube-shaped cellular constructs fashioned from crosslinked collagen and bone marrow stromal cells were found to have burst pressures significantly higher than their non-crosslinked analogs (71 +/- 4 mmHg vs. 46 +/- 3 mmHg; p < 0.01). Thus, the transglutaminase mediated reaction served to successfully strengthen collagen gels while remaining benign toward cells. (C) 2004 Wiley Periodicals, Inc.