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.
Much attention has been paid to the natural mechanism of silkworm spinning due to the impressive mechanical 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 nucleation-dependent aggregation mechanism, which is similar to that found in Prion protein (PrP) denaturation and Aβ-peptide aggregations, leading to the neurodegenerative disease. This work would help one understand further the natural spinning process of silkworm. Additionally, it would be significant 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 denaturation and Aβ-peptide aggregations.
关键词
丝绸
蚕丝蛋白
构象转换
铜离子
环分色性
silk fibroin, conformational transition, Cu(Ⅱ) ions, circular dichroism.