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引起白内障的S78F和S78P突变的γD-晶体蛋白降低蛋白质的结构稳定性和驱动聚合.

Ningqin Lin1, Ying Zhang2, Xiaohui Song3

  • 1Department of Nephrology, The Children's Hospital, Zhejiang University School of Medicine, National Clinical Research Center for Child Health, Hangzhou, Zhejiang Province, China; Eye Center of the Second Affiliated Hospital, Zhejiang University School of Medicine, 88 Jiefang Road, Hangzhou 310009, China; Institute of Translational Medicine, Zhejiang University School of Medicine, 268 Kaixuan Road, Hangzhou 310020, China.

International journal of biological macromolecules
|September 22, 2023
PubMed
概括
此摘要是机器生成的。

在玛D晶体中的两个先天性白内障突变破坏了透镜蛋白质结构,并导致聚合. 兰醇可以逆转这些聚合物,提供对儿童失明机制的见解.

关键词:
出生性白内障是一种先天性白内障.兰醇的使用方法蛋白质聚合蛋白质的聚合.蛋白质的稳定性 蛋白质的稳定性γD-晶素的使用.

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科学领域:

  • 分子生物学分子生物学
  • 生物化学 生物化学
  • 眼科医生 眼科 眼科

背景情况:

  • 先天性白内障是儿童失明的主要原因,通常是基因驱动的.
  • 玛D晶体 (γD-crystallin) 对透镜透明度至关重要,突变可能导致白内障.
  • 许多γD-晶突变的致病机制尚不清楚.

研究的目的:

  • 研究两种导致白内障的γD晶体突变的结构和聚合机制:Ser78Phe (S78F) 和Ser78Pro (S78P).
  • 探索保存的Ser78残留在维护γD晶体稳定性中的作用.
  • 评估兰醇在逆转突变诱导的蛋白质聚合中的潜力.

主要方法:

  • 使用光光谱学,圆形二元化 (CD) 和尺寸排除色谱 (SEC) 净化和结构性表征野生类型 (WT) 和突变的γD-晶体.
  • 在细菌 (大肠杆菌) 和哺乳动物细胞系 (HLE-B3,HEK 293T) 中表达突变,以研究蛋白质溶解性和侵袭性细胞的形成.
  • 在环境压力下对聚合的研究和评估兰醇的逆转效应.
  • 分子动态模拟用于分析分子层面的结构变化.

主要成果:

  • 与WT γD-crystallin.相比,S78F和S78P突变均表现出降低溶解度,增加水性暴露,以及降低热稳定性.
  • 突变物的过度表达诱导了细胞系中的侵略性形成,聚合因热量,紫外线和氧化应激而加剧.
  • 兰醇治疗逆转了细胞内S78F和S78P聚合物.
  • 分子动力学模拟显示,这两种突变都破坏了希腊键动机2的完整性.

结论:

  • 保存的Ser78残留物对于保持γD晶体结构稳定性至关重要.
  • S78F和S78P突变使蛋白质不稳定,导致聚合和潜在的白内障形成.
  • 兰醇显示出逆转晶体聚合的潜力,为某些类型的白内障提供治疗见解.