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钛基和钴基生物材料的表面预处理对纤维状胶原蛋白共价固定化的影响。

Influence of surface pretreatment of titanium- and cobalt-based biomaterials on covalent immobilization of fibrillar collagen.

作者信息

Müller Rainer, Abke Jochen, Schnell Edith, Scharnweber Dieter, Kujat Richard, Englert Carsten, Taheri Darius, Nerlich Michael, Angele Peter

机构信息

Institute of Physical and Theoretical Chemistry, University of Regensburg, Universitätsstrasse 31, 93053 Regensburg, Germany.

出版信息

Biomaterials. 2006 Aug;27(22):4059-68. doi: 10.1016/j.biomaterials.2006.03.019. Epub 2006 Mar 31.

Abstract

Collagen type-I is a major component of the extracellular matrix of most tissues and it is increasingly utilized for surface engineering of biomaterials to accelerate receptor-mediated cell adhesion. In the present study, coatings with layers of fibrillar type-I collagen were prepared on titanium, titanium alloy, and cobalt alloy to improve initial osteoblast adhesion and implant-tissue integration. To suppress the quick in vivo degradation rate of collagen the deposited layers were covalently immobilized at the metal surfaces as well as chemically cross-linked. The application of different oxidation techniques to the metallic substrates resulted in surfaces with varying hydroxyl group contents, which directly influenced the amount of immobilized silane coupling agents. It was found that a high density of surface-bound coupling agents increased the stability of the covalently linked collagen layers. After coating of metallic biomaterials with a cross-linked collagen layer, an improved cellular response of human osteoblast-like cells (MG-63) in vitro could be recognized.

摘要

I型胶原蛋白是大多数组织细胞外基质的主要成分,并且越来越多地用于生物材料的表面工程,以加速受体介导的细胞粘附。在本研究中,在钛、钛合金和钴合金上制备了具有I型原纤维胶原蛋白层的涂层,以改善成骨细胞的初始粘附和植入物与组织的整合。为了抑制胶原蛋白在体内的快速降解率,沉积层在金属表面进行了共价固定以及化学交联。对金属基材应用不同的氧化技术导致表面具有不同的羟基含量,这直接影响了固定化硅烷偶联剂的量。结果发现,高密度的表面结合偶联剂增加了共价连接的胶原蛋白层的稳定性。在用交联胶原蛋白层涂覆金属生物材料后,可以识别出体外人成骨样细胞(MG-63)的细胞反应得到改善。

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