Overexpression of the Bcl-2
protein has emerged as a hallmark of
carcinoma cells and can be employed as a biochemical
biomarker of these cells. Therefore, some Bcl-2
protein fluorescence probes (BPFPs) were designed for Bcl-2
protein quantification and
carcinoma cells labeling. The high Bcl-2 protein binding affinity (Ki < 1 nM) and selectivity (over 50,000-fold Bcl-2
protein selectivity against Mcl-1
protein) of BPFP1 endow it with the ability to detect trace amounts of Bcl-2
protein. After being incubated with a range of concentrations of Bcl-2
protein, BPFP1 exhibited the desired fluorescence properties and its fluorescence intensity is proportional to Bcl-2
protein concentration. Therefore, BPFP1 provides a convenient approach for Bcl-2
protein quantification and we could determine the concentration of Bcl-2
protein based on the BPFP1's fluorescence intensity. Subsequent studies revealed that BPFP1 can fluorescently label
carcinoma cells by binding to overexpressed Bcl-2
protein in living cells, and can distinguish
carcinoma cells (HL-60 cells and ACHN cells) from normal-tissue cells (HUVECs) according to the different Bcl-2
protein expression levels between
carcinoma cells and normal tissue cells. In the present study, BPFP1 represents a new tool for Bcl-2
protein quantification,
carcinoma cell visualization and cell sorting. Moreover, BPFP1 can be used in the future for early
cancer diagnosis by detecting
carcinoma cells in patient tissues.