Pre-incubation under high pressure accelerates amyloid formation from insulin

被引:1
作者
Fujimoto, Y [1 ]
Tanaka, N [1 ]
Kunugi, S [1 ]
机构
[1] Kyoto Inst Technol, Dept Polymer Sci & Engn, Sakyo Ku, Kyoto 6068585, Japan
关键词
insulin; amyloid; high pressure; protein; denaturation; aggregation;
D O I
10.1295/polymj.38.302
中图分类号
O63 [高分子化学(高聚物)];
学科分类号
070305 ; 080501 ; 081704 ;
摘要
Some fundamental high pressure effects on β-amyloid formation from insulin were investigated. The amyloid formation process was observed by adding fluorescent probe, thioflavine T 20mM, in the insulin solutions. It was observed that high pressure suppressed the amyloid formation of insulin and both nucleation and extension were slowed down by giving high pressure. The main mechanism of pressure retardation of amyloid formation might be the suppression of both nuclear formation and further aggregation of modified monomer to extend the amyloid fibrils. The results show that the mechanism of the association of the fluorescent probes and the fibrils was also modified by changing the pre-incubating conditions.
引用
收藏
页码:302 / 305
页数:4
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