Evaluation of adhesion force and binding affinity of phytohemagglutinin erythroagglutinating to egf receptor on human lung cancer cells
Journal
Current Medicinal Chemistry
Journal Volume
20
Journal Issue
19
Pages
2476-2485
Date Issued
2013
Author(s)
Abstract
PHA-E is a natural product extracted from red kidney beans, and it has been reported to induce cell apoptosis by blocking EGFR in lung cancer cells. Because EGF is the major in vivo competitor to PHA-E in clinical application, PHA-E must be proved that has better affinity to EGFR than EGF. This study would focus on how PHA-E tightly bind to EGFR and the results would compare with EGF. The adhesion force, measured by AFM, between EGFR and PHA-E was 207.14±74.42 pN that was higher than EGF (183.65±86.93 pN). The equilibrium dissociation constant of PHA-E and EGF to EGFR was 2.4×10 -9±1.4×10-9 and 7.3×10 -8±2.7×10-8, respectively, that could evaluate binding affinity. The result showed that binding affinity of PHA-E to EGFR was one order higher than EGF to EGFR. In the results of flow cytometer and confocal microscope, we found binding efficiency of EGF to EGFR was decrease as the concentration of PHA-E increased. In the analysis of Western blot, treatment of A-549 cells with PHA-E resulted in a dose-dependent decrease in EGFR phosphorylation. In conclusion, we found that PHA-E had better adhesion force and binding affinity to EGFR than that of the EGF. The interaction between PHA-E and EGFR could block EGF binding and then inhibit EGFR phosphorylation. PHA-E could be developed into a new target molecule for lung cancer treatment that could be immobilized on the drug carrier to guide therapeutic particles to the tumor site. ? 2013 Bentham Science Publishers.
Subjects
Adhesion force; Binding affinity; Epidermal growth factor receptor; Lung cancer; Natural product; Phytohemagglutinin erythroagglutinating; Target molecule
SDGs
Other Subjects
epidermal growth factor; epidermal growth factor receptor; phytohemagglutinin; phytohemagglutinin erythroagglutinating; unclassified drug; article; atomic force microscopy; binding affinity; cancer cell; confocal microscopy; flow cytometry; human; human cell; lung cancer; Western blotting; Antineoplastic Agents, Phytogenic; Cell Line, Tumor; Epidermal Growth Factor; Humans; Lung Neoplasms; Phosphorylation; Phytohemagglutinins; Protein Binding; Receptor, Epidermal Growth Factor
Type
journal article