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Cu(II) effect on the conformation of regenerated silk fibroin in dilute aqueous solution

Cu(II) effect on the conformation of regenerated silk fibroin in dilute aqueous solution

作     者:ZONG Xiaohong ZHOU Ping SHAO Zhengzhong WANG Honghai CHUNYU Lijuan 

作者机构:The Key Laboratory of Molecular Engineering of Polymers Ministry of education Department of Macromolecular Science Fudan University Shanghai 200433 China Institute of Genetics Fudan University Shanghai 200433 China 

出 版 物:《Chinese Science Bulletin》 (Chin. Sci. Bull.)

年 卷 期:2005年第50卷第17期

页      面:1859-1863页

核心收录:

学科分类:0821[工学-纺织科学与工程] 08[工学] 082102[工学-纺织材料与纺织品设计] 

基  金:National Natural Science Foundation of China  NSFC  (20274009  29974004) 

主  题:丝绸 蚕丝蛋白 构象转换 铜离子 环分色性 

摘      要:Much attention has been paid to the natural mechanism of silkworm spinning due to the impressive me-chanical properties of the natural fibers. In this work, we studied the effect of Cu(II) ions on the secondary structure of Bombyx mori regenerated silk fibroin (SF) in dilute solution by circular dichroism (CD). The results indicate that a given amount of Cu(II) induces the SF conformational transition from random coil to β-sheet, however, further addition of Cu(II) is unfavorable for this conversion. Meanwhile, the conformational changes induced by Cu(II) follow a nuclea-tion-dependent aggregation mechanism, which is similar to that found in Prion protein (PrP) denaturation and Aβ-pep- tide aggregations, leading to the neurodegenerative disease. This work would help one understand further the natural spinning process of silkworm. Additionally, it would be sig-nificant for the study of the nervous system diseases, because silk fibroin, extracted in large amounts from Bombyx mori silkworm gland, could be a proper model to study PrP dena-turation and Aβ-peptide aggregations.

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