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CT200 is a first-in-class, 13-amino acid cell-penetrating peptide derived from the C-terminal domain of β-tubulin. It specifically targets and inhibits the chaperonin-containing TCP-1 (CCT) complex, a protein-folding machine that is often overexpressed in cancer cells to manage the high demand for folding cytoskeletal proteins like actin and tubulin. By interfering with CCT-mediated protein folding, CT200 induces proteostatic stress, disrupts the cytoskeleton, and triggers apoptosis, particularly in aggressive cancers like triple-negative breast cancer (TNBC). Developed by Cureteq, CT200 represents a novel approach to targeting the protein-folding machinery of the cell, offering a potential therapeutic strategy for tumors that are resistant to standard-of-care treatments.
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