AMCF-RDP:一个基于自注意的多源级联框架,用于识别药物-蛋白质关系。

IF 3.8 2区 化学 Q2 CHEMISTRY, APPLIED
Zhanchao Li, Xiaoyu Li, Xiuli Tang, Yan Wang
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引用次数: 0

摘要

确定药物与蛋白质之间的关系不仅有助于病理机制的研究,而且有助于药物重新定位的研究。然而,传统的湿实验室方法经常受到诸如耗时,劳动密集型和精度低等问题的困扰。因此,发展一种理论计算方法对于快速准确地鉴定药物-蛋白质关系是必要的。本研究建立了一个基于自我注意的多源级联框架(AMCF-RDP)来识别药物-蛋白质关系。利用知识图谱和复杂网络衍生的嵌入特征和网络拓扑特征来表征药物-蛋白质关系。利用注意机制和全连接层构建了两层模型,用于预测药物是否与蛋白质相互作用以及相互作用的类型。基于非冗余数据集、消融实验以及与机器学习算法和其他最先进方法的比较,对所提出方法的有效性进行了评估和确认。五重交叉验证结果表明,该方法能够快速准确地识别药物-蛋白质相互作用,准确率为90.21%,灵敏度为90.35%,马修斯相关系数为0.8043。此外,它还可以区分药物-蛋白相互作用的类型,宏观召回率为93.43%,宏观f1得分为0.9381。与文献中描述的方法相比,本文方法的受试者工作特征曲线下面积为0.9176,提高了0.4746。共鉴定出10万个药物-蛋白关联,其中一些通过分子对接、KEGG和基因本体分析得到证实。AMCF-RDP已被证明可以显著提高药物-蛋白质关系的鉴定。预计这将成为药物开发和研究作用机制领域的宝贵工具。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
AMCF-RDP: a self-attention-based multi-source and cascade framework for the identification of drug-protein relationships.

The identification of relationships between drugs and proteins not only helps in the study of pathological mechanisms but also in drug repositioning studies. However, conventional wet-lab methods are often plagued by issues such as being time-consuming, labour-intensive, and characterized by low accuracy. Therefore, the development of a theoretical computational method is imperative for the expeditious and precise identification of drug-protein relationships. In this study, a self-attention-based multi-source and cascade framework (AMCF-RDP) is developed to identify the drug-protein relationships. Embedded features and network topology features derived from the knowledge graph and complex network were employed to characterize the drug-protein relationships. A two-layer model was constructed using attention mechanism and fully connected layers and was used to predict whether a drug interacts with a protein and what type of interaction it is. The efficacy of the proposed method was evaluated and confirmed based on the non-redundant datasets, ablation experiments, and comparisons with machine learning algorithms and other state-of-the-art methods. Results from fivefold cross-validation demonstrate that the developed method can quickly and accurately recognize drug-protein interactions with an accuracy of 90.21%, a sensitivity of 90.35%, and a Matthews correlation coefficient of 0.8043. Furthermore, it can also distinguish the types of drug-protein interaction, achieving a macro-recall of 93.43% and a macro-F1 score of 0.9381. Compared to the methods described in the literature, the proposed method achieved an area under the receiver operating characteristic curve of 0.9176, representing an improvement of 0.4746. A total of 100,000 drug-protein associations were identified, some of which were confirmed through molecular docking, KEGG, and gene ontology analyses. The AMCF-RDP has been demonstrated to significantly improve the identification of drug-protein relationships. It is anticipated that this will serve as a valuable tool in the domains of drug development and the investigation of mechanisms of action.

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来源期刊
Molecular Diversity
Molecular Diversity 化学-化学综合
CiteScore
7.30
自引率
7.90%
发文量
219
审稿时长
2.7 months
期刊介绍: Molecular Diversity is a new publication forum for the rapid publication of refereed papers dedicated to describing the development, application and theory of molecular diversity and combinatorial chemistry in basic and applied research and drug discovery. The journal publishes both short and full papers, perspectives, news and reviews dealing with all aspects of the generation of molecular diversity, application of diversity for screening against alternative targets of all types (biological, biophysical, technological), analysis of results obtained and their application in various scientific disciplines/approaches including: combinatorial chemistry and parallel synthesis; small molecule libraries; microwave synthesis; flow synthesis; fluorous synthesis; diversity oriented synthesis (DOS); nanoreactors; click chemistry; multiplex technologies; fragment- and ligand-based design; structure/function/SAR; computational chemistry and molecular design; chemoinformatics; screening techniques and screening interfaces; analytical and purification methods; robotics, automation and miniaturization; targeted libraries; display libraries; peptides and peptoids; proteins; oligonucleotides; carbohydrates; natural diversity; new methods of library formulation and deconvolution; directed evolution, origin of life and recombination; search techniques, landscapes, random chemistry and more;
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