...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>The FEBS journal >Protein oligomerization induced by oleic acid at the solid-liquid interface - equine lysozyme cytotoxic complexes
【24h】

Protein oligomerization induced by oleic acid at the solid-liquid interface - equine lysozyme cytotoxic complexes

机译：油酸在固液界面诱导的蛋白质低聚-马溶菌酶细胞毒性复合物

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

Protein oligomeric complexes have emerged as a major target of current research because of their key role in aggregation processes in living systems and in vitro. Hydrophobic and charged surfaces may favour the self-assembly process by recruiting proteins and modifying their interactions. We found that equine lysozyme assembles into multimeric complexes with oleic acid (ELOA) at the solid-liquid interface within an ion-exchange chromatography column preconditioned with oleic acid. The properties of ELOA were characterized using NMR, spectroscopic methods and atomic force microscopy, and showed similarity with both amyloid oligomers and the complexes with oleic acid and its structural homologous protein l-lactalbumin, known as humanl-lactalbumin made lethal for tumour cells (HAMLET). As determined by NMR diffusion measurements, ELOA may consist of 4-30 lysozyme molecules. Each lysozyme molecule is able to bind 11-48 oleic acids in various preparations. Equine lysozyme acquired a partially unfolded conformation in ELOA, as evident from its ability to bind hydrophobic dye 8-anilinonaphthalene-1-sulfonate. CD and NMR spectra. Similar to amyloid oligomers, ELOA also interacts with thioflavin-T dye, shows a spherical morphology, assembles into ring-shaped structures, as monitored by atomic force microscopy, and exerts a toxic effect in cells. Studies of well-populated ELOA shed light on the nature of the amyloid oligomers and HAMLET complexes, suggesting that they constitute one large family of cytotoxic proteinaceous species. The hydrophobic surfaces can be used profitably to produce complexes with very distinct properties compared to their precursor proteins.
机译：蛋白质寡聚复合物已经成为当前研究的主要目标，因为它们在生命系统和体外的聚集过程中起着关键作用。疏水和带电荷的表面可通过募集蛋白质并修饰其相互作用来促进自组装过程。我们发现马溶菌酶在油酸预处理的离子交换色谱柱内的固液界面处与油酸（ELOA）组装成多聚体复合物。 ELOA的特性使用NMR，光谱法和原子力显微镜进行了表征，并显示出与淀粉样蛋白低聚物以及与油酸及其结构同源蛋白l-乳白蛋白（称为人乳白蛋白）的复合物的相似性，该蛋白对肿瘤细胞具有致命性（HAMLET ）。如通过NMR扩散测量所确定的，ELOA可以由4-30个溶菌酶分子组成。每个溶菌酶分子都能够在各种制剂中结合11-48油酸。从其结合疏水染料8-苯胺基萘-1-磺酸盐的能力可以看出，马溶菌酶在ELOA中获得了部分展开的构象。 CD和NMR谱。类似于淀粉样蛋白低聚物，ELOA还与硫代黄素-T染料相互作用，显示出球形形态，组装成环形结构（通过原子力显微镜观察），并在细胞中发挥毒性作用。人口稠密的ELOA的研究揭示了淀粉样蛋白低聚物和HAMLET复合物的性质，表明它们构成了细胞毒性蛋白物种的一个大家族。与它们的前体蛋白相比，疏水表面可以有利地用于生产具有非常不同特性的复合物。

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