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Sensors 2015, 15(8), 19429-19442; doi:10.3390/s150819429

Electrochemical Characterization of Protein Adsorption onto YNGRT-Au and VLGXE-Au Surfaces

1
Department of Chemistry, Oakland University, 2200 North Squirrel Road, Rochester, MI 48309, USA
2
Faculty of Pharmacy and Pharmaceutical Sciences, University of Alberta, 87 Avenue, Edmonton, AB T6G 2E1, Canada
3
Chapman University School of Pharmacy, Harry and Diane Rinker Health Science Campus, Chapman University, Irvine, CA 92618-1908, USA
*
Author to whom correspondence should be addressed.
Academic Editor: Kagan Kerman
Received: 27 June 2015 / Revised: 30 July 2015 / Accepted: 2 August 2015 / Published: 7 August 2015
View Full-Text   |   Download PDF [1248 KB, uploaded 7 August 2015]   |  

Abstract

The adsorption of the proteins CD13, mucin and bovine serum albumin on VLGXE-Au and YNGRT-Au interfaces was monitored by electrochemical impedance spectroscopy in the presence of [Fe(CN)6]3−/4−. The hydrophobicity of the Au surface was tailored using specific peptides, blocking agents and diluents. The combination of blocking agents (ethanolamine or n-butylamine) and diluents (hexanethiol or 2-mercaptoethanol) was used to prepare various peptide-modified Au surfaces. Protein adsorption onto the peptide-Au surfaces modified with the combination of n-butylamine and hexanethiol produced a dramatic decrease in the charge transfer resistance, Rct, for all three proteins. In contrast, polar peptide-surfaces induced a minimal change in Rct for all three proteins. Furthermore, an increase in Rct was observed with CD13 (an aminopeptidase overexpressed in certain cancers) in comparison to the other proteins when the VLGXE-Au surface was modified with n-butylamine as a blocking agent. The electrochemical data indicated that protein adsorption may be modulated by tailoring the peptide sequence on Au surfaces and that blocking agents and diluents play a key role in promoting or preventing protein adsorption. The peptide-Au platform may also be used for targeting cancer biomarkers with designer peptides. View Full-Text
Keywords: peptides; CD13; mucin; electrochemistry peptides; CD13; mucin; electrochemistry
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Trzeciakiewicz, H.; Esteves-Villanueva, J.; Soudy, R.; Kaur, K.; Martic-Milne, S. Electrochemical Characterization of Protein Adsorption onto YNGRT-Au and VLGXE-Au Surfaces. Sensors 2015, 15, 19429-19442.

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