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首页> 外文期刊>RSC Advances >Digging deeper: structural background of PEGylated fibrin gels in cell migration and lumenogenesis
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Digging deeper: structural background of PEGylated fibrin gels in cell migration and lumenogenesis

机译：挖掘更深：聚乙二醇化纤维蛋白凝胶的结构背景在细胞迁移和漏洞发生中

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摘要

Fibrin is a well-known tool in tissue engineering, but the structure of its modifications created to improve its properties remains undiscussed despite its importance, e.g. in designing biomaterials that ensure cell migration and lumenogenesis. We sought to uncover the structural aspects of PEGylated fibrin hydrogels shown to contribute to angiogenesis. The analysis of the small-angle X-ray scattering (SAXS) data and ab initio modeling revealed that the PEGylation of fibrinogen led to the formation of oligomeric species, which are larger at a higher PEG?:?fibrinogen molar ratio. The improvement of optical properties was provided by the decrease in aggregates' sizes and also by retaining the bound water. Compared to the native fibrin, the structure of the 5?:?1 PEGylated fibrin gel consisted of homogenously distributed flexible fibrils with a smaller space between them. Moreover, as arginylglycylaspartic acid (RGD) sites may be partly bound to PEG-NHS or masked because of the oligomerization, the number of adhesion sites may be slightly reduced that may provide the better cell migration and formation of continuous capillary-like structures.
机译：纤维蛋白是一种众所周知的组织工程工具，但尽管重要的是，其为改善其特性而产生的修改的结构仍未讨论，例如，它仍然是未致辞的。在设计生物材料方面，确保细胞迁移和疏液相生。我们试图揭示所示出有助于血管生成的Pegymated纤维蛋白水凝胶的结构方面。小角X射线散射（SAXS）数据和AB初始建模的分析表明，纤维蛋白原的聚乙二醇化导致寡聚物种的形成，其在更高的PEGα：β纤维蛋白原摩尔比。通过将聚集体的尺寸的减少提供了光学性质的改善，并且还通过保持结合的水。与天然纤维蛋白相比，5的结构？：1聚乙二醇化纤维蛋白凝胶由均质分布的柔性原纤维组成，它们之间的空间较小。此外，由于氨基丙基天冬氨酸（RGD）位点可以部分地与PEG-NHS或掩蔽的位点部分地结合或由于寡聚化而掩蔽，可以略微降低粘合位点的数量，其可以提供更好的细胞迁移和形成连续毛细管样结构。

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