Previous studies have demonstrated that
interleukin-11 (IL-11) and the
IL-11 receptor (IL-11R) are associated with the regulation of
tumor progression and may play a significant role in bone
metastases. The nonapeptide structure c(CGRRAGGSC) is a phage display-selected
IL-11 mimic, which binds to IL-11R. The aim of this study is to investigate the binding characteristics of a cyclic nonapeptide c(CGRRAGGSC) in LNCaP human
prostate cancer cells. To investigate its binding and uptake effects, c(CGRRAGGSC) was labeled with a
fluorescent dye, LSS670. The binding location of LSS670 cyclic nonapeptide in LNCaP cells was investigated by fluorescence microscopy. Flow cytometry was used to detect the fluorescence of LSS670-c(CGRRAGGSC) in LNCaP cells. The binding of LSS670-c(CGRRAGGSC) in LNCaP cells was inhibited by unlabeled cyclic nonapeptide, depending on the varying density of c(CGRRAGGSC) and different time points. The
molecular probe bound to the LNCaP cell membrane and cytoplasm through fluorescence tracing. In the saturation experiments performed in vitro, the K(d) value was 3.2±0.02 nM and the B(max) value was 754±34 fmol/mg.pro. The 50% inhibiting concentration (IC(50)) was 6.31±0.12 nmol/l and the K(i) value was 2.11±0.14 nmol/l in competitive inhibition experiments. Our results suggest that c(CGRRAGGSC) is able to specifically bind to LNCaP cells through a receptor-mediated pathway.