重组 Dragline Silk-Like 蛋白--表达和纯化。

IF 0.1 4区 工程技术 Q4 CHEMISTRY, APPLIED
Aatcc Review Pub Date : 2011-03-01
William A Gaines, William R Marcotte
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引用次数: 0

摘要

蜘蛛拖丝是一种蛋白质纤维,具有令人印象深刻的物理特性,因此非常适合用于先进材料。这种纤维由两种蛋白质(蜘蛛丝蛋白 MaSp1 和 MaSp2)组成,每种蛋白质都包含一个大的中央重复阵列,两侧是非重复的 N 端和 C 端结构域。重复阵列似乎在很大程度上决定了纤维的拉伸特性,这表明 N 端和 C 端结构域可能参与了自组装。我们最近从 Nephila clavipes 中分离出了 MaSp1 和 MaSp2 N 端结构域,并将其整合到迷你蚕丝基因中,以便在转基因系统中表达。目前的工作包括开发表达载体,以便使用可移除的亲和标签纯化蛋白质,从而实现可扩展的蛋白质纯化。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Recombinant Dragline Silk-Like Proteins-Expression and Purification.

Spider dragline silk is a proteinaceous fiber with impressive physical characteristics making it attractive for use in advanced materials. The fiber is composed of two proteins (spidroins MaSp1 and MaSp2), each of which contains a large central repeat array flanked by non-repetitive N- and C-terminal domains. The repeat arrays appear to be largely responsible for the tensile properties of the fiber, suggesting that the N- and C-terminal domains may be involved in self-assembly. We recently isolated the MaSp1 and MaSp2 N-terminal domains from Nephila clavipes and have incorporated these into mini-silk genes for expression in transgenic systems. Current efforts involve the development of expression vectors that will allow purification using a removable affinity tag for scalable protein purification.

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Aatcc Review
Aatcc Review 工程技术-材料科学:纺织
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