溶菌酶
化学
淀粉样蛋白(真菌学)
动力学
淀粉样变性
无定形固体
蛋清
淀粉样纤维
蛋白质聚集
生物物理学
结晶学
淀粉样β
生物化学
生物
无机化学
病理
物理
医学
量子力学
疾病
作者
Sian-Yang Ow,Dave E. Dunstan
出处
期刊:Soft Matter
[The Royal Society of Chemistry]
日期:2013-01-01
卷期号:9 (40): 9692-9692
被引量:71
摘要
Lysozyme is associated with hereditary systemic amyloidosis in humans. Hen egg white lysozyme (HEWL) has been extensively studied as an amyloid forming protein. In this study, we investigated HEWL amyloid formation over a range of temperatures at two stirring speeds and at low concentrations to avoid gel formation. The amyloid fibril formation was found to follow first order kinetics with the rate determining step being the unfolding of the lysozyme. Both the rate of formation and final amount of amyloid formed show maxima with temperature at approximately at 65 °C. CD measurements show that the lysozyme is unfolded by 55 °C. The decrease in amyloid formation at temperatures above 65 °C is attributed to competing amorphous aggregation. The majority of the non-fibrillar aggregates are small and uniform in size with a few larger amorphous aggregates observed in the AFM images.
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