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首页> 外文期刊>Acta biomaterialia >Immobilization of a phosphonated analog of matrix phosphoproteins within cross-linked collagen as a templating mechanism for biomimetic mineralization.
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Immobilization of a phosphonated analog of matrix phosphoproteins within cross-linked collagen as a templating mechanism for biomimetic mineralization.

机译：将基质磷酸化蛋白的磷酸化类似物固定在交联胶原蛋白中，作为仿生矿化的模板机制。

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Immobilization of phosphoproteins on a collagen matrix is important for the induction of intrafibrillar apatite mineralization. Unlike phosphate esters, polyphosphonic acid has no reactive sites for covalent binding to collagen amine groups. Binding of poly(vinyl phosphonic acid) (PVPA), a biomimetic templating analog of matrix phosphoproteins, to collagen was found to be electrostatic in nature. Thus, an alternative retention mechanism was designed for immobilization of PVPA on collagen by cross-linking the latter with carbodiimide (EDC). This mechanism is based on the principle of size exclusion entrapment of PVPA molecules within the internal water compartments of collagen. By cross-linking collagen with EDC, a zero length cross-linking agent, the sieving property of collagen is increased, enabling the PVPA to be immobilized within the collagen. The absence of covalent cross-linking between PVPA and collagen was confirmed by Fourier transform infrared spectroscopy. Based on these results, a concentration range for immobilized PVPA to template intrafibrillar apatite deposition was established and validated using a single layer reconstituted type I collagen mineralization model. In the presence of a polyacrylic acid-containing mineralization medium optimal intrafibrillar mineralization of the EDC-cross-linked collagen was achieved using 500 and 1000 mug ml(1) PVPA. The mineralized fibrils exhibited a hierarchical order of intrafibrillar mineral infiltration, as manifested by the appearance of electron-dense periodicity within unstained fibrils. Understanding the basic processes in intrafibrillar mineralization of reconstituted collagen creates opportunities for the design of tissue engineering materials for hard tissue repair and regeneration.
机译：将磷蛋白固定在胶原蛋白基质上对于诱导原纤维内磷灰石矿化很重要。与磷酸酯不同，多膦酸没有反应位点可与胶原胺基共价结合。发现聚（乙烯基膦酸）（PVPA）（一种基质磷蛋白的仿生模板类似物）与胶原蛋白的结合本质上是静电的。因此，设计了另一种保留机制，通过将PVPA与碳二亚胺（EDC）交联将PVPA固定在胶原上。该机制基于胶原内部水腔室中PVPA分子的尺寸排阻截留原理。通过将胶原蛋白与零长度交联剂EDC交联，可以提高胶原蛋白的筛分性能，从而使PVPA固定在胶原蛋白内。通过傅立叶变换红外光谱法证实了PVPA和胶原之间不存在共价交联。基于这些结果，建立了固定的PVPA到模板的原纤维内磷灰石沉积的浓度范围，并使用单层重构的I型胶原矿化模型进行了验证。在含有聚丙烯酸的矿化介质的存在下，使用500和1000毫升ml（1）PVPA可以实现EDC交联胶原蛋白的最佳原纤维内矿化。矿化的原纤维表现出原纤维内矿物质渗透的等级顺序，这由未染色的原纤维内电子致密周期性的出现所证明。了解重构胶原蛋白的纤维内矿化的基本过程为组织工程材料的设计提供了机会，以进行硬组织修复和再生。

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