作为热休克蛋白90（Hsp90）抑制剂的杂环化合物的分子对接和药效团研究
Molecular docking and pharmacophore studies of heterocyclic compounds as Heat shock protein 90 (Hsp90) Inhibitors.
作者信息
Baby Suby T, Sharma Shailendra, Enaganti Sreenivas, Cherian P Roby
机构信息
Faculty of Pharmaceutical Sciences, Jodhpur National University, Jodhpur, Rajasthan 342003, India.
Bioinformatics division, Averin biotech, Nallakunta, Hyderabad, Telangana 500044, India.
出版信息
Bioinformation. 2016 Jun 15;12(3):149-155. doi: 10.6026/97320630012149. eCollection 2016.
Heat Shock Protein 90 was a key molecular chaperone involved in the proteome stability maintenance and its interference in many signaling networks associated with cancer progression, makes it of an important target for cancer therapeutics. The present study aimed to identify potential lead molecule among the selected heterocyclic compounds against Human Hsp90 (PDB: 1YET) through docking using GOLD 3.1 and pharmacophore studies using Discovery studio 2.1. On the basis of the GOLD Fitness scores, the compounds Q1G and T21 showed better binding affinity. Further the analyzed structure pharmacophore results are in consistence with the docking results indicating that both these compounds show antagonistic activity towards HSP90 respectively.
热休克蛋白90是一种关键的分子伴侣，参与蛋白质组稳定性的维持，并且它对许多与癌症进展相关的信号网络产生干扰，这使其成为癌症治疗的重要靶点。本研究旨在通过使用GOLD 3.1进行对接以及使用Discovery studio 2.1进行药效团研究，在所选杂环化合物中鉴定针对人热休克蛋白90（PDB：1YET）的潜在先导分子。基于GOLD适应度评分，化合物Q1G和T21表现出更好的结合亲和力。此外，分析的结构药效团结果与对接结果一致，表明这两种化合物分别对热休克蛋白90表现出拮抗活性。
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