biostudies-literatureZhang FU.S. Department of Health and Human ServicesNational Natural Science Foundation of ChinaNIGMS NIH HHSNatural Science Foundation of Jiangsu Province9960-5https://www.ebi.ac.uk/biostudies/studies/S-EPMC4836855biostudies-literatureUnknown87(19)Epidermal growth factor receptor (EGFR, also known as ErbB-1 or HER-1) is a membrane bound protein that has been associated with a variety of solid tumors and the control of cell survival, proliferation, and metabolism. Quantification of the EGFR expression level in cell membranes and the interaction kinetics with drugs are thus important for cancer diagnosis and treatment. Here we report mapping of the distribution and interaction kinetics of EGFR in their native environment with the surface plasmon resonance imaging (SPRi) technique. The monoclonal anti-EGFR antibody was used as a model drug in this study. The binding of the antibody to EGFR overexpressed A431 cells was monitored in real time, which was found to follow the first-order kinetics with an association rate constant (ka) and dAnalytical chemistryQuantification of epidermal growth factor receptor expression level and binding kinetics on cell surfaces by surface plasmon resonance imaging.PMC48368551R44GM106579-01R44 GM106579R01 GM107165BK20140592R44 GM1267201R01GM107165-01A121405080Zhang FGuan YYang YWang SWang WXu HYin LTao NfalseQuantification of epidermal growth factor receptor expression level and binding kinetics on cell surfaces by surface plasmon resonance imaging.Epidermal growth factor receptor (EGFR, also known as ErbB-1 or HER-1) is a membrane bound protein that has been associated with a variety of solid tumors and the control of cell survival, proliferation, and metabolism. Quantification of the EGFR expression level in cell membranes and the interaction kinetics with drugs are thus important for cancer diagnosis and treatment. Here we report mapping of the distribution and interaction kinetics of EGFR in their native environment with the surface plasmon resonance imaging (SPRi) technique. The monoclonal anti-EGFR antibody was used as a model drug in this study. The binding of the antibody to EGFR overexpressed A431 cells was monitored in real time, which was found to follow the first-order kinetics with an association rate constant (ka) and d2015-01-01T00:00:00Z2015 Oct2026-05-05T16:47:10.935Z2019-03-27T02:11:56ZS-EPMC48368552636833410.1021/acs.analchem.5b02572