Malignant cells are dependent on novel activated form of molecular chaperone
A newly identified biochemical difference between malignant cells and normal cells points to a novel molecular target for the development of selective anti-cancer drugs, according to research published today in the journal Nature by scientists from Conforma Therapeutics. Conforma scientists have shown that Heat-Shock Protein 90 (Hsp90), a molecular "chaperone" that maintains the stability and functional shape of many oncogenic signaling proteins, exists in a specific activated, high-affinity form in tumor cells that differs from the "resting" form of Hsp90 found in normal cells. This novel, activated Hsp90 explains the selectivity of Hsp90 inhibitors for tumor cells, including compounds identified by Conforma that bind to tumor-derived Hsp90 with 100-fold greater affinity than to Hsp90 derived from normal cells.
"This discovery explains why Hsp90-directed drugs kill tumor cells at doses that are not toxic to normal tissues," said Lawrence C. Fritz, Ph.D., president and chief executive officer of Conforma Therapeutics and an author of the paper. "We hope to begin testing our ideas and compounds in human clinical trials early next year."
Joan Kureczka | EurekAlert!
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