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GF9 is a first-in-class, ligand-independent peptide inhibitor of Triggering Receptor Expressed on Myeloid cells 1 (TREM-1). Developed using the Signaling Chain Homo-Oligomerization (SCHOOL) strategy, GF9 is designed to disrupt the structural assembly and homodimerization of the TREM-1 signaling complex rather than competing for its ligand-binding site. This mechanism effectively blocks TREM-1-mediated signaling in myeloid cells, such as tumor-associated macrophages (TAMs), which are known to promote tumor growth, metastasis, and an immunosuppressive microenvironment. Preclinical studies have shown that GF9 administration can significantly attenuate tumor growth, reduce TAM infiltration, and prolong survival in models of pancreatic cancer and non-small cell lung cancer (NSCLC). The peptide has been evaluated both in its free form and as part of lipopeptide complexes intended to extend its half-life and improve targeted delivery.
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