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MP30:Miniature Electronic Biosensor for the Detection of Glycan Biomarkers

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Poster Author Names and Affiliations

1. Vinay J Nagaraj: Center for Bioelectronics and Biosensors, The Biodesign Institute at Arizona State University

2. Manish Bothara: Portland State University

3. Seron Eaton: Center for Bioelectronics and Biosensors, The Biodesign Institute at Arizona State University

4. Peter Wiktor: Center for Bioelectronics and Biosensors, The Biodesign Institute at Arizona State University

5. Shalini Prasad: Wichita State University


Poster Title

Miniature Electronic Biosensor for the Detection of Glycan Biomarkers

Poster Abstract

Glycans (oligosaccharide chains attached to proteins) hold great promise as a new class of biomarkers for the early diagnosis of cancer and other diseases. To realize the potential of glycans as biomarkers and to overcome the inherent limitations of current laboratory analytical techniques, we are developing a novel ultrasensitive diagnostic platform called ‘NanoMonitor’ to enable rapid label-free glycosylation analysis from human samples in a clinical setting. The operation of the NanoMonitor is based on the principles of electrochemical impedance spectroscopy. The device consists of a silicon chip with an array of gold electrodes forming multiple sensor sites. Each sensor site is overlaid with a nanoporous alumina membrane that forms a high density of nanowells. Lectins, proteins that bind to and recognize specific glycan structures, are conjugated to the surface of the electrode. A perturbation to the electrical double-layer is produced when specific glycoproteins from a test sample bind to lectins at the base of each nanowell. This perturbation results in a change in the impedance of the double layer. In order to test the ability of NanoMonitor to identify defined glycan structures, as well as distinguish between closely related ones, we analyzed glycoform variants of the serum protein fetuin for binding to a panel of lectins on the NanoMonitor. The highly specific binding pattern of lectins to fetuin glycoforms on the NanoMonitor correlated very well with results from a conventional laboratory technique (ELISA). However, compared to ELISA, the analysis of protein glycosylation was quick (about 10 min), completely label free, required just 10 µl of sample, and was several orders of magnitude more sensitive. Analysis of protein extracts from cultured human pancreatic cells on the NanoMonitor indicated the presence of significantly higher amount of α-(2,3) linked rather than α-(2,6) linked sialic acids. Our results indicate that the NanoMonitor is capable of rapid label-free protein glycosylation analysis with high sensitivity and selectivity over a broad dynamic range of glycoprotein concentrations. This system can be easily integrated into a handheld electronic instrument for use as a point-of-care diagnostic device for routine detection of glycan biomarkers from clinical samples.

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