Binding sites for luminescent amyloid biomarkers from non-biased molecular dynamics simulations,Chemical Communications

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Binding sites for luminescent amyloid biomarkers from non-biased molecular dynamics simulations
Chemical Communications ( IF 4.3 ) Pub Date : 2018-03-01 00:00:00 , DOI: 10.1039/c8cc00105g
Carolin König _{1,

2,

3,

4} , Robin Skånberg _{4,

5,

6,

7} , Ingrid Hotz _{4,

5,

6,

7} , Anders Ynnerman _{4,

5,

6,

7} , Patrick Norman _{1,

2,

3,

4} , Mathieu Linares _{1,

2,

3,

4,

8}

Affiliation

A very stable binding site for the interaction between a pentameric oligothiophene and an amyloid-β(1–42) fibril has been identified by means of non-biased molecular dynamics simulations. In this site, the probe is locked in an all-trans conformation with a Coulombic binding energy of 1200 kJ mol⁻¹ due to the interactions between the anionic carboxyl groups of the probe and the cationic ε-amino groups in the lysine side chain. Upon binding, the conformationally restricted probes show a pronounced increase in molecular planarity. This is in line with the observed changes in luminescence properties that serve as the foundation for their use as biomarkers.

中文翻译：

来自无偏分子动力学模拟的发光淀粉样生物标志物的结合位点

通过无偏分子动力学模拟，已经确定了五聚体寡噻吩与淀粉样β（1-42）原纤维之间相互作用的非常稳定的结合位点。在该位置，由于探针的阴离子羧基与赖氨酸侧链中的阳离子ε-氨基之间的相互作用，探针以1200 kJ mol ^-1的库仑结合能被锁定为全反式构象。结合后，构象受限的探针显示出分子平面度的显着增加。这与所观察到的发光性质变化相一致，这些变化为它们用作生物标记物奠定了基础。

更新日期：2018-03-21

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