豐富的魚類蛋白可抑制α-突觸核蛋白澱粉樣蛋白形成

論文標題：Abundant fish protein inhibits α-synuclein amyloid formation

期刊：Scientific Reports

作者：Tony Werner, Ranjeet Kumar, Istvan Horvath, Nathalie Scheers, Pernilla Wittung-Stafshede

發表時間：2018/04/03

數字識別碼： 10.1038/s41598-018-23850-0

原文連結：http://t.cn/ELRNZJD

魚類體內最常見的過敏原是β-小清蛋白，這種蛋白質在魚體內含量豐富，能夠形成澱粉樣結構以避免胃腸道降解並進入血液。在人類中，相同的澱粉樣蛋白結構主要與神經退行性疾病如阿爾茨海默症、帕金森症有關。近日Scientific Reports發表的研究Abundant fish protein inhibits α-synuclein amyloid formation對這些澱粉樣蛋白之間的可能聯繫進行了探究。

來自瑞典查爾姆斯理工大學的Pernilla Wittung-Stafshede及其團隊使用的是重組大西洋鱈魚β-小清蛋白和帕金森病中的主要澱粉樣蛋白——α-突觸核蛋白。通過一系列體外生物物理方法，研究人員發現β-小清蛋白能抑制α-突觸核蛋白形成澱粉樣蛋白。實現這種抑制的背後機制是α-突觸核蛋白會與β-小清蛋白澱粉樣蛋白纖維表面相結合。

除了這種全新的澱粉樣蛋白抑制機制外，研究數據還表明，β-小清蛋白與人體澱粉樣蛋白的交叉反應也可部分解釋食用魚肉帶來的健康益處。

圖1：不同的蛋白分別形成澱粉樣蛋白結構的ThT螢光圖(a)和AFM圖(b)。

摘要：The most common allergen in fish, the highly-abundant protein β-parvalbumin, forms amyloid structures as a way to avoid gastrointestinal degradation and transit to the blood. In humans, the same amyloid structures are mostly associated with neurodegenerative disorders such as Alzheimer’s and Parkinson’s. We here assessed a putative connection between these amyloids using recombinant Atlantic cod β-parvalbumin and the key amyloidogenic protein in Parkinson’s disease, α-synuclein. Using a set of in vitro biophysical methods, we discovered that β-parvalbumin readily inhibits amyloid formation of α-synuclein. The underlying mechanism was found to involve α-synuclein binding to the surface of β-parvalbumin amyloid fibers. In addition to being a new amyloid inhibition mechanism, the data suggest that health benefits of fish may be explained in part by cross-reaction of β-parvalbumin with human amyloidogenic proteins.

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期刊介紹：Scientific Reports (https://www.nature.com/srep/) is an online, open access journal from the publishers of Nature. We publish scientifically valid primary research from all areas of the natural and clinical sciences.

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（來源：科學網）

 

 

 

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