PBP10

PBP10 is a cell-permeable, rhodamine-B-conjugated peptide derived from the polyphosphoinositide-binding domain (residues 160–169) of the human protein gelsolin. It functions as a selective antagonist of the Formyl Peptide Receptor 2 (FPR2), also known as the Lipoxin A4 (LXA4) receptor or ALX. By inhibiting FPR2, PBP10 blocks the signaling effects of LXA4 and other pro-inflammatory or pro-tumorigenic agonists. In oncological research, PBP10 has been shown to interfere with the polarization of tumor-associated macrophages (TAMs) toward an M2-like phenotype by preventing LXA4-mediated inhibition of METTL3, thereby reducing the tumorigenicity of prostate cancer cells. Beyond its receptor-antagonist properties, PBP10 is also known to sequester phosphatidylinositol 4,5-bisphosphate (PIP2), which can disrupt various intracellular signaling pathways and cellular processes such as actin remodeling and neutrophil activation.

Other names

Rhodamine-B-QRLFQVKGRRgelsolin-derived peptide PBP10Rhodamine-B-conjugated gelsolin-derived peptide