Current Topics in Medicinal Chemistry

Allen B. Reitz
Fox Chase Chemical Diversity Center, Inc.
Doylestown, PA


Pharmacological Targeting of the Hsp70 Chaperone

Author(s): Srikanth Patury, Yoshinari Miyata and Jason E. Gestwicki

Affiliation: University of Michigan, Life Sciences Institute, 210 Washtenaw Ave, Ann Arbor, MI 48109-2216.


The molecular chaperone, heat shock protein 70 (Hsp70), acts at multiple steps in a proteins life cycle, including during the processes of folding, trafficking, remodeling and degradation. To accomplish these various tasks, the activity of Hsp70 is shaped by a host of co-chaperones, which bind to the core chaperone and influence its functions. Genetic studies have strongly linked Hsp70 and its co-chaperones to numerous diseases, including cancer, neurodegeneration and microbial pathogenesis, yet the potential of this chaperone as a therapeutic target remains largely underexplored. Here, we review the current state of Hsp70 as a drug target, with a special emphasis on the important challenges and opportunities imposed by its co-chaperones, protein-protein interactions and allostery.

Keywords: Proteostasis, flavonoids, dihydropyrimidines, spergualin, sulfoglycolipids, geranylgeranyl acetone, protein folding, ATPase, protein-protein interactions

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Article Details

Page: [1337 - 1351]
Pages: 15
DOI: 10.2174/156802609789895674
Price: $58