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Preparation and Characterization of Antherea pernyi silk fibroin scaffold for tissue engineering

机译:组织工程用百日红蚕丝素蛋白支架的制备与表征

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Silk fibroin from Antheraea pernyi (A. pernyi), one of wild silkworms, has different primary structure and mechanical properties from that of domestic silkworm Bombyx mori (B.mori). The primary structure of A. pemyi silk fibroin is consisted of the repeated similar sequences by about 100 times where there are alternative appearance of polyalanine ( PLA) region , (Ala)12-13 and Gly-rich region. Interestingly, the sequence RGD, which is the adhesion motif from fibronectin on extracellular matrix (ECM) proteins, is found in the primary structure of A. pernyi silk fibroin. This implies that A. pernyi fibroin has surface for cell attachment when it is processed as scaffolds in tissue engineering.Therefore, this study tried to find out the potential application of A. pernyi silk fibroin in the field of tissue engineering. The processing ability, biomineralization and cell activity of A. pernyi silk fibroin were investigated. Film was formed by using HFA as solvent. As shown in Figure 1, hydroapatite crystals were formed on A.pernyi silk fibroin through absorbed in 1.5 SBF solution, proving that A.pernyi silk fibroin hasbiomineralized ability. A.pernyi silk fibroin also shows cell adhesion and growth activities in response to NHDF. Therefore, it seems that A.pernyi silk fibroin has potential application as scaffolds in the field of tissue engineering.
机译:野生蚕Antheraea pernyi(A. pernyi)的丝素蛋白与家蚕Bombyx mori(B.mori)具有不同的主要结构和机械性能。 pemyi丝素蛋白的一级结构由重复的相似序列组成,约为100倍,其中有聚丙氨酸(PLA)区,(Ala)12-13和富含Gly的区域交替出现。有趣的是,在pernyi丝素蛋白的一级结构中发现了RGD序列,它是纤连蛋白在细胞外基质(ECM)蛋白上的粘附基序。这暗示着,pernyi丝素蛋白在组织工程中被用作支架时具有细胞附着的表面。因此,本研究试图发现pernyi丝素蛋白在组织工程领域中的潜在应用。研究了per蚕丝素蛋白的加工能力,生物矿化和细胞活性。使用HFA作为溶剂形成膜。如图1所示,在1.5 SBF溶液中吸收吸附后,在珀氏i丝素蛋白上形成了水合磷灰石晶体,证明了珀氏i丝素蛋白具有 生物矿化能力。 pernyi丝素蛋白还显示出对NHDF的细胞粘附和生长活性。因此,似乎pernyi丝素蛋白在组织工程领域中具有作为支架的潜在应用。

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