Abstract：Abstract: Dragline silk is the strongest of all the spider silks, with superior biocompatibility and biodegradability, which makes it a hot area in biomaterial research. The inadequate understanding of the Araneus ventricosus (A.v.) major ampullate spidroin (MaSp) structure and fiber formation mechanism restricts its bionic application. Herein, A.v. MaSp1, one of the main components of dragline silk, was studied. The full-length N-terminal (NT) coding sequence of A.v. MaSP1 was obtained by anchored PCR, and through gene cloning, expression and purification, the NT protein was harvested at a yield of 60 mg/L. Meanwhile, the C-terminal (CT) of MaSp1 was also expressed and purified with a yield of 80 mg/L. The secondary structures of MaSp1 NT and CT were determined from CD spectra and the curves showed that α-helix is the main structure of both proteins. The results set the foundation for the research of structure and fiber formation mechanism of A.v. MaSp1.
引用本文:
贾秋品, 温 睿, 李 雪, 孟 清. 大腹园蛛主壶腹腺蛛丝蛋白末端结构域的克隆表达[J]. 生命科学研究, 2019, 23(3): 200-207. JIA Qiu-pin, WEN Rui, LI Xue, MENG Qing. Cloning and Expression of Terminal Domains of MaSp from Araneus ventricosus. Life Science Research, 2019, 23(3): 200-207.
