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首页> 外文期刊>Australian Journal of Dairy Technology >The two-faced nature of milk casein proteins: amyloid fibril formation and chaperone-like activity
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The two-faced nature of milk casein proteins: amyloid fibril formation and chaperone-like activity

机译：酪蛋白乳蛋白的两面性：淀粉样原纤维形成和伴侣蛋白样活性

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摘要

Molecular chaperones are a diverse group of proteins that stabilise partially folded target proteins to prevent their misfolding, aggregation and potential precipitation under conditions of cellular stress, e.g. elevated temperature. Protein aggregation, particularly the formation of highly ordered protein aggregates termed amyloid fibrils, is of considerable research interest because of its intimate association with a wide range of debilitating diseases, including Alzheimer's, Parkinson's and Huntington's diseases and type II diabetes. In this review, we discuss the ability of the milk casein proteins to act in a chaperone-like manner. This property is of biological importance since at least two of the casein proteins, alpha(S2)- and kappa-casein, have a propensity to assemble into amyloid fibrils under physiological conditions. The fibril-forming propensity of alpha(s2)- and kappa-casein, the possibility of its occurrence in mammary tissue, and the ability of the other casein proteins, alpha(s1)- and beta-casein, to inhibit the aggregation of alpha(s2)- and kappa-casein and other proteins, are discussed. The results have application in the use of casein proteins in a systematic manner to stabilise other proteins at high temperature and under shear conditions, as occurs in the industrial treatment of milk and milk-based products.
机译：分子伴侣是一类多样化的蛋白质，可以稳定部分折叠的目标蛋白质，以防止它们在细胞压力（例如细胞压力）条件下的错误折叠，聚集和潜在的沉淀。高温。蛋白质聚集，特别是称为淀粉样蛋白原纤维的高度有序的蛋白质聚集的形成，由于与许多衰弱性疾病（包括阿尔茨海默氏病，帕金森氏病和亨廷顿氏病和II型糖尿病）密切相关，因此引起了广泛的研究兴趣。在这篇综述中，我们讨论了酪蛋白乳蛋白以伴侣蛋白样方式起作用的能力。该性质具有生物学重要性，因为至少两种酪蛋白蛋白质，α（S2）-和κ-酪蛋白在生理条件下具有组装成淀粉样原纤维的倾向。 α（s2）-和κ-酪蛋白的原纤维形成倾向，其在乳腺组织中发生的可能性以及其他酪蛋白蛋白质α（s1）-和β-酪蛋白抑制α聚集的能力（s2）-和κ-酪蛋白和其他蛋白质，进行了讨论。该结果以系统的方式应用于酪蛋白的应用，以稳定其他蛋白质在高温和剪切条件下的稳定性，就像在牛奶和基于牛奶的产品的工业处理中一样。

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