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TAT-HA-stathmin wild-type peptide
- Development stage
- Preclinical
- Lead developer
- Icahn School of Medicine
- Modality
- Peptides
- Administration
- Parenteral
01
Overview
TAT-HA-stathmin wild-type peptide is a synthetic cell-penetrating peptide designed to inhibit microtubule assembly and cell proliferation in breast cancer. The peptide consists of a short stathmin-like domain derived from the N-terminal region of the microtubule-destabilizing protein stathmin, fused to a TAT transduction domain (which acts as a cell-penetrating carrier) and a hemagglutinin (HA) epitope tag for intracellular tracking. By mimicking stathmin's N-terminal domain, the peptide binds to tubulin and impedes tubulin polymerization, thereby disrupting microtubule dynamics and inhibiting the proliferation of breast cancer cells. It was developed by researchers at the Mount Sinai School of Medicine.
- Other names
- TAT-HA-stathmin wild-type
02
Targets
TUBB (Tubulin (alpha and beta subunits))
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