靶向Aurora A激酶:通过综合药效团和模拟方法计算发现有效抑制剂。

Bhuvaneswari Sivaraman, Kathiravan Muthukumaradoss
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引用次数: 0

摘要

癌症目前是全球第二大最常见的死亡原因,主要是由于异常有丝分裂过程驱动的不受控制的细胞生长。Aurora A激酶(AURKA)是有丝分裂的关键调控因子,参与中心体成熟、双极性纺锤体形成和细胞分裂,已被确定为有希望的抗癌靶点。本研究采用综合计算方法来鉴定新的AURKA抑制剂。利用MOE软件,以6种有效的AURKA抑制剂为基础,建立了基于配体的药效团模型。该模型由aro /HydA、Acc和Don/Acc三个特征组成,阈值为80 %,具有很强的判别能力,灵敏度为69.8 %,特异性为63.6 %,准确率为60.4 %。锌数据库的筛选产生了774个命中,其中A1 (ZINC63106872)和A2 (ZINC39272872)被确定为最佳候选,与参考MK-5108 (-7.49 kcal/mol)相比,它们具有更高的对接分数(-9.24和-8.97 kcal/mol)。这些命中符合利平斯基规则,并表现出有利的ADMET特征。DFT分析显示,偶极矩增大(A1: 6.15 D, A2:6.39 D), HOMO-LUMO间隙减小(A1: 0.33 eV, A2: 0.38 eV),表明极性和反应性增强。MEP图显示了两种化合物明确的供体-受体区,具有平衡的表面。超过500 ns的分子动力学模拟证实了复合物的稳定性,蛋白质骨架RMSD约为2.8 Å,配体RMSD为4.0 Å (A1)和6.0 Å (A2)。RMSF值保持在2.4以下Å。在MM-GBSA分析中,A1的结合能最有利(-75.34 kcal/mol),证实了其强相互作用和治疗潜力。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Targeting Aurora A kinase: Computational discovery of potent inhibitors through integrated pharmacophore and simulation approaches.

Cancer currently ranks as the second most common cause of mortality worldwide, primarily due to uncontrolled cell growth driven by aberrant mitotic processes. Aurora A kinase (AURKA), a key regulator of mitosis involved in centrosome maturation, bipolar spindle formation, and cytokinesis, has been identified as a promising anticancer target. This study employs a comprehensive computational approach to identify new AURKA inhibitors. Using MOE software, a ligand-based pharmacophore model was developed based on six potent AURKA inhibitors. The model, consisting of three features-Aro/HydA, Acc, and Don/Acc-at an 80 % threshold, demonstrated strong discriminative power with a sensitivity of 69.8 %, specificity of 63.6 %, and accuracy of 60.4 %. Screening of the ZINC database yielded 774 hits, from which A1 (ZINC63106872) and A2 (ZINC39272872) were identified as the top candidates, with superior docking scores (-9.24 and -8.97 kcal/mol) compared to the reference MK-5108 (-7.49 kcal/mol). These hits satisfied Lipinski's rule and exhibited favourable ADMET profiles. DFT analysis revealed higher dipole moments (A1: 6.15 D, A2:6.39 D) and narrower HOMO-LUMO gaps (A1: 0.33 eV, A2: 0.38 eV), indicating enhanced polarity and reactivity. MEP plots showed defined donor-acceptor zones for both compounds, having a balanced surface. Molecular dynamics simulations over 500 ns confirmed complex stability, with protein backbone RMSD around 2.8 Å and ligand RMSD of 4.0 Å (A1) and 6.0 Å (A2). RMSF values remained below 2.4 Å. The most favourable binding energy for A1 (-75.34 kcal/mol) in MM-GBSA analysis confirms its strong interaction and therapeutic potential.

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