• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Australian Journal of Dairy Technology >Protective interactions of dairy peptides with fibril structures and relevance to Alzheimer's Disease
【24h】

Protective interactions of dairy peptides with fibril structures and relevance to Alzheimer's Disease

机译：乳肽与原纤维结构的保护性相互作用以及与阿尔茨海默氏病的相关性

获取原文
获取原文并翻译 | 示例
       
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Selected dairy caseins have been shown to have capacity for chaperone-like regulation of folding pathways of other caseins, specifically in preventing development of fibrillar aggregates of beta sheet structure. An assay based on fibril formation by reduced and carboxymethylated-kappa casein (RCM-kCn) was thus used to screen for anti-fibril activity among a selection of dairy protein hydrolysates, in order to discover peptides with possible anti-fibril, chaperone activity. From the selection of eight dairy hydrolysates based on different dairy protein fractions, two of the hydrolysates of whey protein exhibited superior anti-fibril bioactivity against RCM-kCn and amyloid beta (A beta), the peptide associated with fibrillar plaque deposits in brains of Alzheimer's Disease patients. It is also possible that the chaperone-like activity responsible for anti-fibril activity may exert protective bioactivity in other protein folding diseases involving proteins other than A beta, accessible from the periphery. Anti-fibril peptides may also confer stability and prevent aggregation of thermally denatured dairy protein systems during processing. These results demonstrate the capacity of dairy peptides to inhibit A beta fibril formation in vitro and justifies further investigation of this property as a novel class of bioactivity for dairy peptides.
机译：已显示出所选的酪蛋白酪蛋白具有对其他酪蛋白的折叠途径进行伴侣状调节的能力，特别是在防止β片层结构的原纤维聚集体发展方面。因此，基于还原和羧甲基化酪蛋白酪蛋白（RCM-kCn）的原纤维形成的测定用于筛选乳制品蛋白水解产物中的原纤维活性，以发现具有可能的原纤维，伴侣蛋白活性的肽。从基于不同乳蛋白组分的八种乳制品水解物中选择，乳清蛋白的两种水解物显示出对RCM-kCn和淀粉样蛋白β（A beta）（与阿尔茨海默氏病大脑中与纤维斑块相关的肽）的抗原纤维生物活性。疾病患者。负责抗原纤维活性的类似伴侣分子的活性也可能在涉及从外周进入的涉及除Aβ以外的蛋白质的其他蛋白质折叠疾病中发挥保护性生物活性。抗原纤维肽还可以赋予稳定性并防止在加工过程中热变性乳蛋白系统的聚集。这些结果证明了乳肽在体外抑制Aβ原纤维形成的能力，并且证明了对该特性作为乳肽的新型生物活性的进一步研究的合理性。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号