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HEAT SHOCK PROTEINS: A BETTER TARGET IN PREVENTION OF CANCER

Journal Name:

  • The International Journal of Pharmaceutical Research and Bio-Science

Publication Year:

  • 2013

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Abstract (2. Language): 
Heat shock protein-90 is an energy dependent molecular chaperone involved in folding and stabilizing of various oncogenic client proteins to their active conformations that makes it promising anti-cancer target. Heat shock protein-90 inhibitors attacks at amino and carboxyl -terminal ATP pocket of molecule for the antitumor response. The clinical development of Heat shock protein-90 inhibitors from Geldanamycin and their analogues like Tanespimycin, Alvespinycin, Retaspimycin and newest agents till now has revealed miraculous encouraging results in field of acute myeloid leukemia, refractory prostate cancer, small cell lung carcinoma and breast cancer. Others derivatives of purine, resorcinol, indazolone have also a point of attraction. These categories of compounds will continuously driven forward by the optimization of pharmaceutical properties including pharmacokinetic, pharmacodynamic and toxicological in clinical studies with time. This class of compounds principally inhibits the ATPase activity of chaperon by to the N and C-terminal of chaperon. There are a multitude of second generation inhibitors currently under investigatory clinical trials. Till date, there is neither any FDA approved any heat shock protein-90 inhibitors nor standardized assay to ascertain inhibition. This review summarizes the current status of both first and second generation heat shock protein-90 inhibitors based on their chemical classification and stage of clinical development. Ultimately, these efforts will aid in maximizing the biological and pharmacological knowledge of potential of this class.
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