Effect of L-thyroxine, a Human Serum Albumin Natural Ligand, on the Kinetics of β-amyloid Peptide Fibril Formation

E. Litus, E. Nemashkalova, A. A. Vologzhannikova, E. Deryusheva
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Abstract

Ligands of human serum albumin (HSA) are capable of modulating its interaction with β-amyloid peptide (Aβ), which is a key factor in the pathogenesis of Alzheimer’s disease (AD). L-thyroxine (L-Tr), a natural HSA ligand, is associated with the pathogenesis of AD according to epidemiological and animal model studies. In this work, we studied the kinetics of Aβ fibril formation in the presence of L-Tr and HSA using a fluorescent test with thioflavin T. L-Tr had no significant effect on the inhibitory effect of HSA on fibril growth. At the same time, L-Tr itself had an inhibitory effect similar to that of HSA. Our data can partially explain the relationship between AD and thyroid pathologies.
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人血清白蛋白天然配体 L-甲状腺素对 β 淀粉样肽纤维形成动力学的影响
人血清白蛋白(HSA)的配体能够调节其与β-淀粉样肽(Aβ)的相互作用,而β-淀粉样肽是阿尔茨海默病(AD)发病机制中的一个关键因素。根据流行病学和动物模型研究,天然 HSA 配体 L-甲状腺素(L-Tr)与阿尔兹海默病的发病机制有关。在这项工作中,我们使用硫黄素 T 荧光测试法研究了在 L-Tr 和 HSA 存在下 Aβ 纤维的形成动力学。同时,L-Tr 本身的抑制作用与 HSA 相似。我们的数据可以部分解释AD与甲状腺病变之间的关系。
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