基于无偏分子动力学模拟的发光淀粉样蛋白生物标志物结合位点研究
Binding Sites for Luminescent Amyloid Biomarkers from non-Biased Molecular Dynamics Simulations
摘要：
五聚体寡聚噻吩和淀粉样蛋白- $β$（1-42）原纤维之间相互作用的一个非常稳定的结合位点已通过无偏分子动力学模拟鉴定。在该位点中，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，探针被锁定在库仑结合能为1，200 kJ/mol的全反式构象中。在结合时，构象限制的探针显示出分子平面性的显著增加。这与观察到的发光性质的变化一致，发光性质的变化是其用作生物标志物的基础。
英文摘要：
A very stable binding site for the interaction between an 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 1,200 kJ/mol 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.
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