The signal transduction pathway initiated by vascular endothelial growth factor-vascular
endothelial growth factor receptor 2 (VEGF-VEGFR2) plays an important role in the angiogenesis of
tumors. The effective antagonists of VEGFR2 would behave as potent drugs for the treatment of
malignant cancers. In our study, specific binding peptides with high affinity to VEGFR2 were obtained through bacterial
display technology. Conserved motif (FF/YEXWGVK) among those peptide sequences was discovered. One of the
selected peptides, VRBP1 (YDGNSFYEMWGVKPASES) was identified by screening the biased bacterial peptide library
and its physiochemical feature was further characterized. The results of surface plasmon resonance (SPR) assay indicated
that the dissociation constant (KD) value of VRBP1 was 228.3 nM and this peptide competed with VEGF binding to
VEGFR2. Particles conjugated with VRBP1 could recognize the human umbilical vein endothelial cells (HUVEC) which
express VEGFR2 on the surface. Further therapeutic effect of VRBP1 was examined by in vivo experiments. VRBP1
could result in a significant decrease in tumor size of H460 xenografts. The results from the immunohistochemical assay
showed that CD31 positive signals in VRBP1-treated group were fewer than those in the control ones. These data
highlighted the potential of VEGFR2-binding peptides as effective molecules for cancer diagnosis and therapy.
Keywords: Angiogenesis, bacterial surface display, cancer diagnosis, cancer therapy, peptide, vascular endothelial growth
factor receptor 2 (VEGFR2).
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