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Electrically Tunable Ultra-specific Zinc Oxide Biosensor

Published online by Cambridge University Press:  06 February 2015

Rujuta D. Munje ,
Andi Wangzhou ,
Anjan Panneer Selvam ,
Sriram Muthukumar  and
Shalini Prasad
Rujuta D. Munje
Affiliation:
Department of Bioengineering, University of Texas at Dallas, 800 W. Campbell Road, EC 39, Richardson, TX 75080, USA
Andi Wangzhou
Affiliation:
Department of Bioengineering, University of Texas at Dallas, 800 W. Campbell Road, EC 39, Richardson, TX 75080, USA
Anjan Panneer Selvam
Affiliation:
Department of Bioengineering, University of Texas at Dallas, 800 W. Campbell Road, EC 39, Richardson, TX 75080, USA
Sriram Muthukumar
Affiliation:
Department of Materials Science and Engineering, University of Texas at Dallas, 800 W. Campbell Road, EC 39, Richardson, TX 75080, USA
Shalini Prasad
Affiliation:
Department of Bioengineering, University of Texas at Dallas, 800 W. Campbell Road, EC 39, Richardson, TX 75080, USA
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Abstract

Zinc oxide surface states can be utilized for ultra-specific detection of biomolecules. The major challenges in using ZnO for bio-sensing are attaining enhanced sensitivity and specificity. In this study, we explore the functionalization of zinc in ZnO through utilizing the thiol bond. The purpose of this study is to demonstrate that the ZnO based sensor is capable of achieving high specificity in presence of competitive surface binding through the thiol bond. The final goal is to design an ultra-specific biosensor to detect low occurring biomolecules. In this study, we have selected cortisol as a stress marker to demonstrate quantification and detection from synthetic sweat. In order to demonstrate ultra-specificity, we have used two competitive thiol based molecules binding to zinc, a linker Dithiobis succinimidyl propionate (DSP) and reducing agent of DSP, Dithiothreitol (DTT). Electrochemical impedance spectroscopy (EIS) is used to quantify the signal obtained through various ratiometric concentrations of DSP and DTT. To validate the EIS study results, inherent fluorescence studies are done by mapping changes in green emission spectrum of ZnO before and after linker functionalization. The optimal combination in terms of highest signal is identified to be of 25mM DTT and 50mM DSP. This is implemented in the experiments performed to calibrate the cortisol concentration in synthetic sweat. This study demonstrates the detection of cortisol antigen in synthetic sweat present within the physiological levels of 8 ng/mL to 140 ng/mL.

Keywords

sputteringsensorbiomedical
Type
Articles
Information
MRS Online Proceedings Library (OPL) , Volume 1720: Symposium D – Materials and Concepts for Biomedical Sensing , 2014 , mrsf14-1720-d05-16
Copyright
Copyright © Materials Research Society 2015 

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References

REFERENCES

Ren, X., Chen, D., Meng, X., Tang, F., Hou, X., Han, D., and Zang, L., J.Colloid Interface Sci. 334, 183–187 (2009).CrossRefGoogle Scholar
Singh, S. P., Arya, S. K., Pandey, P., and Malhotra, B. D., Appl. Phys.Lett.91, (2007).Google Scholar
Sadik, P. W., Pearton, S. J., Norton, D. P., Lambers, E. and Ren, F., J. Appl. Phys.101, (2007).CrossRefGoogle Scholar
Cleveland, W. W., Biochemistry 3, 480–482 (1964).CrossRefGoogle Scholar
Singh, J., Iim, J., Watters, E.J., Whitten, J. E., Soares, J. W., Steeves, D. M., Surf. Sci.609, 183-189 (2013).CrossRefGoogle Scholar
Zhang, G., Shi, C., Han, Z., Shi Jun, J., Fu, Z., Kirm, M. and Zimmerer, G., Chinese Phys. Lett.18, 441-442 (2001).Google Scholar
Panneer Selvam, A., Vattipalli, K. M., and Prasad, S., (IEEE Eng. Med. Biol. Soc. Proc. San Diego, CA, 2012) pp. 3251–3254 Google Scholar
Mattson, G., Conklin, E., Desai, S., Nielander, G., Savage, M. D., and Morgensen, S., Molecular Biology Reports 17, 167–183 (1993).CrossRefGoogle Scholar