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Mutant stathmin-like peptide is an experimental microtubule-depolymerizing peptide developed by researchers at the Mount Sinai School of Medicine. It consists of a short stathmin-like domain fused to a TAT transduction domain for intracellular delivery and a hemagglutinin (HA) epitope tag for tracking. To prevent intracellular inactivation by p34cdc2 kinase-mediated phosphorylation, the peptide features a serine-to-alanine mutation at position 16 (S16A). The peptide acts by binding to free tubulin and promoting microtubule depolymerization, thereby disrupting microtubule assembly and inhibiting the malignant proliferation of cancer cells. It has been investigated in preclinical models of breast cancer, both as a monotherapy and in combination with the chemotherapeutic agent vinblastine.
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