In situ targeting TEM8 via immune response and polypeptide recognition by wavelength-modulated surface plasmon resonance biosensor

• DOI: 10.1038/srep20006
• Publication Date: 2016-01-29T10:51:21Z
• Authors: Yimin Wang; Zewei Luo; Kunping Liu; Jie Wang; Yixiang Duan
• Keywords: Fluoroimmunoassay; Microfilament Proteins; Reproducibility of Results; Receptors, Cell Surface; Biosensing Techniques; 02 engineering and technology; Surface Plasmon Resonance; 01 natural sciences; Article; Antibodies; Neoplasm Proteins; 0104 chemical sciences; 3. Good health; Antibody Specificity; Cell Line, Tumor; Immunoglobulin G; Humans; Peptides; 0210 nano-technology; Protein Binding

AbstractThere is an increasing interest in real-time and in situ monitoring of living cell activities in life science and medicine. This paper reports a whole cell sensing protocol over the interface of Au film coupled in a wavelength-modulated surface plasmon resonance (WMSPR) biosensor. With dual parabolic mirrors integrated in the sensor, the compact and miniaturized instrument shows satisfactory refractive index sensitivity (2220 nm/RIU) and a high resolution of resonance wavelength shift of 0.3 nm to liquid samples. The affinity interactions between the biomarker of human tumor endothelial marker 8 (TEM8) and antibody (Ab) or specific polypeptide (PEP) were firstly introduced to WMSPR biosensor analysis. Both the interaction events of Ab-cell and PEP-cell over the Au film interface can be recognized by the sensor and the balance time of interactions is about 20 min. The concentration range of Ab for quantitative monitoring of the TEM8 expression on human colon carcinoma SW620 cells was investigated. The present low-cost and time-saving method provides a time resolution of binding specificity between Ab/PEP and TEM8 for real-time analysis of antigen on living tumor cell surface.