Tyrosine Photophysics During the Early Stages of β-Amyloid Aggregation Leading to Alzheimer's
Tyrosine Photophysics During the Early Stages of β-Amyloid Aggregation Leading to Alzheimer's
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DOI：
10.1021/acs.jpclett.5b01285
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发表时间：
2015-08-06
影响因子：
5.7
通讯作者：
Vyshemirsky, Vladislav
中科院分区：
文献类型：
--
作者：
Rolinski, Olaf J.;Wellbrock, Thorben;Vyshemirsky, Vladislav
我们通过检测内源性酪氨酸荧光衰减的变化来监测导致阿尔茨海默病的毒性β-淀粉样蛋白低聚物的形成。一种新的方法的基础上的非德拜模型的荧光动力学解决了复杂的基础物理。逐渐消失的非单调的荧光衰减率，在早期阶段的聚集作为较大的，紧密包装的低聚物形成，被解释在酪氨酸肽介电弛豫影响的衰减。结果表明，一种新型的荧光寿命传感的基础上的双激发态/介电弛豫的潜力，在广泛的生物分子的应用。结果还调和以前相互冲突的模型，蛋白质内源性荧光衰减的基础上旋转异构体或介电弛豫说明条件下，两者都是明显的。
We have monitored the formation of toxic beta-amyloid oligomers leading to Alzheimer's disease by detecting changes in the fluorescence decay of intrinsic tyrosine. A new approach based on the non-Debye model of fluorescence kinetics resolves the complexity of the underlying photophysics. The gradual disappearance of nonmonotonic fluorescence decay rates, at the early stages of aggregation as larger, tighter-packed oligomers are formed, is interpreted in terms of tyrosine peptide dielectric relaxation influencing the decay. The results demonstrate the potential for a new type of fluorescence lifetime sensing based on dual excited-state/dielectric relaxation, with application across a broad range of biological molecules. The results also reconcile previously conflicting models of protein intrinsic fluorescence decay based on rotamers or dielectric relaxation by illustrating conditions under which both are manifest.