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TAT-HA-stathmin-S16A mutant peptide is a synthetic, cell-permeable peptide designed to disrupt microtubule assembly and inhibit the proliferation of cancer cells, particularly breast cancer. It consists of a short stathmin-like domain fused to a TAT cell-penetrating peptide transduction domain (which acts as a carrier to facilitate intracellular entry) and a hemagglutinin (HA) epitope tag for tracking. The peptide features a serine-to-alanine mutation at position 16 (S16A), which prevents its inactivation by phosphorylation by p34cdc2 kinase, resulting in a more potent and stable form of the stathmin-like domain. By binding to tubulin, the peptide impedes tubulin polymerization and disrupts the microtubule equilibrium, leading to a marked reduction in microtubule density and inhibition of malignant cell proliferation.
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