Heat Shock Proteins, microRNAs, and Drug Design Studies in MedicinalChemistry

Heat shock proteins (Hsps) are highly conserved chaperone protein family which is responsible for proper folding of newly synthesized and misfolded proteins, cellular signaling, and prevention of protein aggregation. Hsps consist of six major members: small Hsps (<30 kDa), Hsp40 (40 kDa), Hsp60 (60 kDa), Hsp70 (70 kDa), Hsp90 (90 kDa), and Hsp100 (100 kDa). Hsps are found at different parts of the cell (mitochondria, endoplasmic reticulum, cytosol) and their expression level is increased under cellular stress conditions (i.e. malignancy, infection, heavy metals, heat, hypoxia, and oxidative stress). Therefore, expression of high levels of Hsps is related with disease’s pathogenesis.