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Lavendustin A is a small molecule tyrosine kinase inhibitor originally isolated from *Streptomyces griseolavendus*. It acts as a selective, cell-permeable, reversible, and substrate competitive inhibitor of the epidermal growth factor receptor (EGFR) tyrosine kinase and p60c-src kinase with little to no inhibition of protein kinase A or C. It inhibits EGFR-associated tyrosine kinase activity with an IC50 around 11 nM and also inhibits tubulin polymerization. Lavendustin A exhibits antitumor activity by blocking these kinases and angiogenesis pathways. Additionally, it has neuroprotective effects by promoting axonal outgrowth in neurons. The compound competitively inhibits ATP binding at the EGFR site but noncompetitively affects peptide substrate binding. It has been used in research to study tyrosine kinase signaling pathways and cancer cell proliferation[1][3][4][5][8][9].
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