基于集成结构和配体方法的构效关系探索:基于羟肟酸的HDAC抑制剂和细胞毒性药物。

IF 1.8 Q3 PHARMACOLOGY & PHARMACY Turkish Journal of Pharmaceutical Sciences Pub Date : 2023-08-22 DOI:10.4274/tjps.galenos.2022.12269
Ekta Shirbhate, Jaiprakash Pandey, Vijay Kumar Patel, Ravichandran Veerasamy, Harish Rajak
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引用次数: 1

摘要

本研究旨在建立有意义且有效的组蛋白去乙酰化酶(HDAC)抑制剂的定量构效关系(QSAR)模型,并将其理化、位阻和静电特性与抗癌活性联系起来。我们从早期的研究成果中选择了一个数据集。靶标和配体分子从公认的数据库中获取,并纳入关键发现,如分子对接(XP滑翔),电子药效团研究和3D QSAR模型设计研究(阶段)。对接发现分子39对接得分较高,与蛋白结合良好。对偏最小二乘因子5进行三维QSAR分析,R2和Q2值分别为0.9877和0.7142,假设AADRR.139的标准偏差较低,为0.1049。基于计算结果,我们得出结论,分子39是抑制HDAC活性的有效候选物。此外,这些计算方法激励在药理学和医疗保健部门发现新的候选药物。
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Exploration of Structure-Activity Relationship Using Integrated Structure and Ligand Based Approach: Hydroxamic Acid-Based HDAC Inhibitors and Cytotoxic Agents.

The present study aimed to establish significant and validated quantitative structure-activity relationship (QSAR) models for histone deacetylase (HDAC) inhibitors and correlate their physicochemical, steric, and electrostatic properties with their anticancer activity. We have selected a dataset from earlier research findings. The target and ligand molecules were procured from recognized databases and incorporated into pivotal findings such as molecular docking (XP glide), e-pharmacophore study and 3D QSAR model designing study (phase). Docking revealed molecule 39 with better docking score and well binding contact with the protein. 3D QSAR analysis, which was performed for partial least squares factor 5 reported good 0.9877 and 0.7142 as R2 and Q2 values and low standard of deviation: 0.1049 for hypothesis AADRR.139. Based on the computational outcome, it has been concluded that molecule 39 is an effective and relevant candidate for inhibition of HDAC activity. Moreover, these computational approaches motivate to discover novel drug candidates in pharmacological and healthcare sectors.

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来源期刊
CiteScore
3.60
自引率
5.90%
发文量
79
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