Despite aggressive treatment regimes,
glioma remains a largely fatal disease. Current treatment limitations are attributed to the precarious locations within the brain where such
tumors grow, their highly infiltrative nature precluding complete resection and lack of specificity among agents capable of attenuating their growth. Here, we show that in vitro,
glioma cells of diverse origins internalize a
peptide encompassing a
tubulin-binding site (TBS) on the neurofilament
light protein. The internalized
peptide disrupts the microtubule network, inhibits migration and proliferation, and leads to apoptosis. Using an intracerebral transplant model, we show that most, if not all, of these responses to
peptide exposure also occur in vivo. Notably, a single intratumor injection significantly attenuates
tumor growth, while neither
peptide uptake nor downstream consequences are observed elsewhere in the host nervous system. Such preferential uptake suggests that the
peptide may have potential as a primary or supplementary
glioblastoma treatment modality by exploiting its autonomous microtubule-disrupting activity or engaging its capacity to selectively target
glioma cells with other cell-disrupting cargos.