Proteins are metabolic factors to perform biochemical functions. For proper
protein function, these macromolecules must be in their properly folded-native states.
Under stress, cells employ Heat Shock Proteins (Hsps) to overcome this folding
problem. For this reason, Hsp proteins play essential roles in the metabolic processes.
In cancer cells the situation is different than healthy cells. Since the metabolic rates of
cancer cells are faster than that of healthy cells, cancer cells overexpress Hsps to rescue
unfolded proteins to perform biochemical functions. Thus, several research groups have
been focused on Hsps. This protein family consists of several members and interacts
with several cell signaling proteins, kinases, and transcriptional factors. All these
interactions provide key controlling points to inhibit cancer cells and drive them to
apoptosis for therapeutic purposes. Different approaches on Hsp mechanism were
employed for cancer cell inhibition either by interrupting Hsp90-apoptosis inhibitor
protein interactions or by blocking Hsp90-proteasome function. In a similar way,
topoisomerase-Hsp90 interaction was perturbed. Small molecules as well as peptides were employed to inhibit functions of Hsp70 and Hsp27. Several designs were
performed and patented using Hsp cascade and this study summarizes the innovative
patents in the area.
Keywords: Antigenic peptide complex, apoptosis, berberine, cancer, chimeric
peptide, delivering an anticancer agent, heat shock protein targeted therapy,
hepatitis, hepatoma, Hsp27, Hsp70 inhibitors, Hsp90 NTD inhibitors, Hsp90 CTD
inhibitors, oncogenic client proteins, peptides, proteasome, protein folding,
protein-protein interaction inhibitor, secreting modified heat shock protein,
topoisomerase I.