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• W105826260 abstract "Breast cancer is a common malignancy and a lifetime risk among females worldwide. It has been observed that Hsp90 is over expressed in many breast cancer cells. Hsp90 is a highly conserved molecular chaperone and its functions that involve stress response, homeostatic control and assembly of wide range of other chaperones in various biological processes. Hsp90 inhibition has been reported to be a therapeutic approach in breast cancer. In the present investigation, Hsp90 has been docked with co-chaperones, anti-cancer drugs and Hsp90 C-terminal domain has been docked with its inhibitors analogues of novobiocin with the help of Hex 6.3 docking software. The results showed that while Hsp90 has high affinity to bind with Trap1. In order to inhibit Hsp90 a wide range of ligands (anti-cancer drug) were selected and docked by Hex 6.3 keeping ATP as control. Geldanamycin having binding energy -315.36 kcal/mol showed highest inhibition among all. While in order to inhibit Hsp90 C-terminal domain a wide range of ligands were selected and docked by Hex 6.3.Coumermycin having binding energy -395.09 kcal/mol showed highest among all. Due to poor solubility and cytotoxicity results, Novobiocin was modified into fifteen analogues using ChemBioDraw Ultra 13.0. While Analogue 4 found to be the best Hsp90 c-terminal domain inhibitor by Hex 6.3 docking software having binding energy 355.05 kcal/mol." @default.
• W105826260 created "2016-06-24" @default.
• W105826260 creator A5066487719 @default.
• W105826260 date "2013-01-01" @default.
• W105826260 modified "2023-09-26" @default.
• W105826260 title "An in silico approach towards breast cancer therapy using Hsp90 as target" @default.
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• W105826260 hasPublicationYear "2013" @default.
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