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• W72070467 abstract "Breast Cancer has become the second most common threat to the people all over the world. Inhibiting Hsp90 has been considered to be an excellent therapeutic approach in breast cancer where the diseased proteins are directed towards proteasomal degradation pathway. However apart from the inhibitors strong binding to Hsp90, they leave other kinds of disadvantages like solubility, and toxicity problems. In our present investigation, we have developed number of hybrid inhibitor molecules using existing Hsp90-inhibitors to achieve a higher binding potential as well as minimal toxic properties. Thus wide range of hybrid drugs were obtained in-silico and to evaluate their inhibitory potential to Hsp90, docking study was performed against Hsp90. Although docking was done at multiple sites however Lys 112 has been found to be the potential active site for hybrid drugs like H1, H2, H3, H4 and H5 in the N terminal domain of Hsp 90. Among them H1 was found to have the highest docking score of 10.116. The 2D ligand interaction analysis confirmed the involvement of four residues Glutamine 43, Asn 51, Leu 96, Ala 55 and Met 98 at the binding interface. Later we evaluated and analysed the pharmacodynamic profile of existing drugs as well as hybrid drugs and physiochemical parameters were also reported. It was concluded that our designed Hybrid (H1) was found to be the best Hsp 90 inhibitor among all the existing as well as designed drugs in-silico in this study." @default.
• W72070467 created "2016-06-24" @default.
• W72070467 creator A5042270089 @default.
• W72070467 date "2014-05-30" @default.
• W72070467 modified "2023-09-27" @default.
• W72070467 title "Insilico design and evaluation of hybrid Hsp 90 inhibitors for cancer therapy" @default.
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