Apostolakou Avgi E, Douska Dimitra E, Litou Zoi I, Trougakos Ioannis P, Iconomidou Vassiliki A
Section of Cell Biology and Biophysics, Department of Biology, School of Science, National and Kapodistrian University of Athens, Panepistimiopolis, 157 01 Athens, Greece.
Molecules. 2025 Apr 13;30(8):1736. doi: 10.3390/molecules30081736.
Alzheimer's disease (AD) affects an increasing number of people as the human population ages. The main pathological feature of AD, amyloid plaques, consists of the key protein amyloid-β and other co-deposited proteins. These co-deposited proteins and their protein interactors could hold some additional functional insights into AD pathophysiology. For this work, proteins found on amyloid plaques were collected from the AmyCo database. A protein-protein and protein-drug interaction network was constructed with data from the IntAct and DrugBank databases, respectively. In total, there were 12 proteins co-deposited on amyloid plaques that reportedly interact with 513 other proteins and are targets of 72 drugs. These drugs were shown to be almost entirely distinct from the panel of drugs currently approved by the FDA for AD and their corresponding protein targets. In conclusion, this work demonstrates the potential for drug repurposing of drugs that target proteins found in amyloid plaques.
随着人口老龄化，阿尔茨海默病（AD）影响着越来越多的人。AD的主要病理特征——淀粉样斑块，由关键蛋白β-淀粉样蛋白和其他共沉积蛋白组成。这些共沉积蛋白及其蛋白相互作用分子可能为AD病理生理学提供一些额外的功能见解。在这项研究中，从AmyCo数据库收集了在淀粉样斑块上发现的蛋白质。分别利用IntAct和DrugBank数据库的数据构建了蛋白质-蛋白质和蛋白质-药物相互作用网络。总共有12种共沉积在淀粉样斑块上的蛋白质，据报道它们与513种其他蛋白质相互作用，并且是72种药物的靶点。这些药物几乎完全不同于目前美国食品药品监督管理局（FDA）批准用于AD的药物及其相应的蛋白质靶点。总之，这项研究证明了针对淀粉样斑块中发现的蛋白质的药物进行重新利用的潜力。
