Inhibitory effects of 尾-ionone on amyloid fibril formation of 尾-lactoglobulin

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• 作者：Baoliang Ma ; Xiong You ; Fujiao Lu
• 关键词：尾-Lactoglobulin ; Amyloid fibrils ; Lag time ; 尾-Ionone ; Protein stability
• 刊名：International Journal of Biological Macromolecules
• 出版年：March, 2014
• 年：2014
• 卷：64
• 期：Complete
• 页码：162-167
• 全文大小：934 K

文摘

尾-Lactoglobulin (尾-LG) is the major constituent of whey food, which has been shown to interact with a wide range of aroma compounds. In the present work, a model aroma compound, 尾-ionone, is used to investigate the influence of aroma compounds on the urea-induced unfolding of 尾-LG at pH 7.0. 尾-Ionone is observed to enhance the stability of 尾-LG at pH 7.0. Moreover, the amyloid fibrils are observed when 尾-LG at pH 7.0 is incubated for 12-20 days at 37 掳C in the presence of 3-5 M urea. However, the formation of amyloid fibrils is inhibited when 尾-ionone is added into the samples and the inhibitory effects follow a concentration-dependent fashion. There is a clear correlation between C_m and lag time. The correlation demonstrates that protein stability affects the amyloid fibril formation of 尾-LG. The results highlight the critical role of protein stability and provide an approach to prevent the formation of amyloid fibrils in vitro.