Microbial production of amino acid-modified spider dragline silk protein with intensively improved mechanical properties

Microbial production of amino acid-modified spider dragline silk protein with intensively improved mechanical properties
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微生物生产氨基酸修饰的蜘蛛丝蛋白,机械性能显着改善

DOI:
10.1080/10826068.2015.1084637
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发表时间:
2016-08
影响因子:
2.9
通讯作者:
Liu Huizhou
Liu Huizhou
中科院分区:
工程技术4区
文献类型:
--
作者:
Zhang Haibo;Zhou Fengli;Jiang Xinglin;Cao Mingle;Wang Shilu;Zou Huibin;Cao Yujin;Xian Mo;Liu Huizhou

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ABSTRACT Spider dragline silk is a remarkably strong fiber with impressive mechanical properties, which were thought to result from the specific structures of the underlying proteins and their molecular size. In this study, silk protein 11R26 from the dragline silk protein of Nephila clavipes was used to analyze the potential effects of the special amino acids on the function of 11R26. Three protein derivatives, ZF4, ZF5, and ZF6, were obtained by site-directed mutagenesis, based on the sequence of 11R26, and among these derivatives, serine was replaced with cysteine, isoleucine, and arginine, respectively. After these were expressed and purified, the mechanical performance of the fibers derived from the four proteins was tested. Both hardness and average elastic modulus of ZF4 fiber increased 2.2 times compared with those of 11R26. The number of disulfide bonds in ZF4 protein was 4.67 times that of 11R26, which implied that disulfide bonds outside the poly-Ala region affect the mechanical properties of spider silk more efficiently. The results indicated that the mechanical performances of spider silk proteins with small molecular size can be enhanced by modification of the amino acids residues. Our research not only has shown the feasibility of large-scale production of spider silk proteins but also provides valuable information for protein rational design.
DOI: 10.1016/s0169-409x(02)00061-3
发表时间: 2002-10
影响因子: 16.1
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发表时间: 1999-12
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