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Published on: June 14, 2012
调节粉样蛋白自我组合和纤维细胞形态与Zn (II)
Jijun Dong1, Jacob E Shokes, Robert A Scott
1Center for the Analysis of SupraMolecular Self-assemblies, Department of Chemistry, Emory University, 1521 Dickey Drive, Atlanta, Georgia 30322, USA.
Journal of the American Chemical Society
|March 16, 2006
概括
离子 (Zn(II)) 在阿贝塔片段中作为粉样蛋白结构的探针. Zn2+ 特别控制自我组装速率和粉样体形态,影响纤维形成和带/管结构.
科学领域:
- 生物化学 生物化学
- 材料科学 材料科学 材料科学
- 结构生物学 结构生物学
背景情况:
- 粉样蛋白结构与各种疾病有关.
- 了解粉样的自我组装对于开发治疗策略至关重要.
- 金属离子可以影响聚和粉样蛋白形成.
研究的目的:
- 研究离子 (Zn(II)) 作为Abeta片段 (Abeta(13-21) 中粉样结构探针的作用.
- 确定Zn2+协调环境如何影响自我组装速度和粉样体形态.
- 为了阐明Zn2+与海斯蒂丁残留物 (His13/His14) 在粉样蛋白形成过程中的特定结合相互作用.
主要方法:
- 射线吸收光谱 (XAS) 用于表征Zn2+协调环境.
- 在Zn2+的存在下研究阿贝塔的自我组装动力学 ((13-21).
- 使用显微镜技术 (隐含) 分析由此产生的粉样体形态.
主要成果:
- Zn2+ 特别控制了阿贝塔的自我组装速率 ((13-21).
- 独特的Zn2+协调环境极大地调节了粉样蛋白形态.
- 在典型的纤维形成中,单一的histidine残留物 (His13) 足以产生Zn2+协调.
- 希斯13/希斯14二极管允许访问不同的Zn2+协调环境,稳定板/板协会,促进带/管的形成.
结论:
- 离子作为有效的探针来了解粉样蛋白的结构和组装.
- Zn2+的协调环境在决定粉样蛋白形态方面发挥着至关重要的作用.
- 在阿贝塔中的特定的伊斯蒂丁残留物中介于基化过程中Zn2+依赖的结构转变.
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