New insight into the mechanism of in vivo fibroin self-assembly and secretion in the silkworm, Bombyx mori
New insight into the mechanism of in vivo fibroin self-assembly and secretion in the silkworm, Bombyx mori
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家蚕体内丝素蛋白自组装和分泌机制的新见解
DOI:
10.1016/j.ijbiomac.2020.12.132
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发表时间:
2021-02-01
影响因子:
8.2
通讯作者:
Zhao, Aichun
中科院分区:
文献类型:
--
作者:
Hao, Zhanzhang;Long, Dingpei;Zhao, Aichun
Fibroin of the silkworm consists of fibroin heavy chain (Fib-H) with hydrophobic intermediate repeats flanked by hydrophilic N and C terminal domains (NTD and CTD, respectively), fibroin light chain (Fib-L), and P25. However, the respective roles of each polypeptide in silk processing remain largely unknown. Here, a series of transgenic silkworms with different fusion gene expression cassettes were created in order to selectively express different fluorescent fusion proteins in silk glands. The roles of different components in silk processing were investigated via observing and analyzing the movement and distribution of these proteins in the silk gland and in cocoon silk. The data showed that hydrophilic NTDs were distributed on the surface of micelles, providing sufficient electrostatic repulsion to prevent premature crystallization of silk proteins. Hydrophilic CTD==Ls ("==" represents the disulfide bond) were located on the inner layer of micelles to control the solubility of large micelles. The results presented here elucidated the underlying mechanisms of silkworm silk processing in vivo. This is significant for the development of artificial spinning technology, novel silk biomaterials, and silk gland expression systems. (C) 2020 Elsevier B.V. All rights reserved.