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Binding of Thioflavin T and Related Probes to Polymorphic Models of Amyloid-β Fibrils
The Journal of Physical Chemistry B ( IF 3.3 ) Pub Date : 2017-09-14 00:00:00 , DOI: 10.1021/acs.jpcb.7b06675
Francesca Peccati 1 , Stefano Pantaleone 1 , Vanessa Riffet 2, 3, 4 , Xavier Solans-Monfort 1 , Julia Contreras-García 2 , Victor Guallar 5, 6 , Mariona Sodupe 1, 6
Affiliation  

Alzheimer’s disease is a challenge of the utmost importance for contemporary society. An early diagnosis is essential for the development of treatments and for establishing a network of support for the patient. In this light, the deposition in the brain of amyloid-β fibrillar aggregates, which is a distinctive feature of Alzheimer, is key for an early detection of this disease. In this work we propose an atomistic study of the interaction of amyloid tracers with recently published polymorphic models of amyloid-β 1–40 and 1–42 fibrils, highlighting the relationship between marker architectures and binding affinity. This work uncovers the importance of quaternary structure, and in particular of junctions between amyloid-β protofilaments, as the key areas for marker binding.

中文翻译:

硫黄素T和相关探针对淀粉样β原纤维多态性模型的绑定。

阿尔茨海默氏病是对当代社会极为重要的挑战。早期诊断对于开发治疗方法以及为患者建立支持网络至关重要。因此,淀粉样蛋白-β纤维状聚集物在大脑中的沉积是阿尔茨海默氏症的一个独特特征,是早期发现该疾病的关键。在这项工作中,我们提出了对淀粉样蛋白示踪剂与最近发表的淀粉样蛋白β1–40和1–42原纤维多态性模型相互作用的原子学研究,强调了标记物结构与结合亲和力之间的关系。这项工作揭示了四级结构的重要性,特别是淀粉样蛋白-β原丝之间的连接作为标志物结合的关键区域的重要性。
更新日期:2017-09-14
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