Biological

Heat Shock Proteins: The Next Target in the Disease Frontier (#91)

Heat shock proteins (Hsps) are molecular chaperones that facilitate protein homoestasis, i.e. the proper folding and function of proteins. In disease states, the function of Hsps are diverted, aiding the advancement of disease rather than appropriately regulating protein turnover in the cell. This makes the Hsps exciting targets in a wide array of therapeutic areas, including Alzheimer’s disease (AD), Huntington’s disease (HD), amyotrophic lateral sclerosis (ALS), cardiovascular disease, and other protein folding disorders. Hsps-related research in Chemistry and Biology is growing rapidly, and a deeper understanding of the heat shock response is leading to numerous potential therapeutic applications for Hsp inhibitors as well as Hsp agonists. In particular, cancer-related treatment options with Hsp90 have already been pursued in the pharmaceutical industry, with numerous lead structures in clinical trials. The importance of Hsp90 in the proper folding and maintenance of proteins has been well documented, and the success of Hsp90 inhibitors in the clinic provides a strong rational for investigating the role of other Hsps. This session will present the latest research on the biology of heat shock proteins, current disease targets, and antagonists and agonists utilized to modulate Hsps and provide new treatment options for a range of diseases.

Last update: Dec 28, 2015