You are not logged in.

Exploring the use of the tripeptide Gly–Gly–His as a selective recognition element for the fabrication of electrochemical copper sensors

Yang, Wenrong, Chow, Edith, Willett, Gary D., Hibbert, D. Brynn and Gooding, J. Justin 2003, Exploring the use of the tripeptide Gly–Gly–His as a selective recognition element for the fabrication of electrochemical copper sensors, Analyst, vol. 128, no. 6, pp. 712-718, doi: 10.1039/B212881K.

Attached Files
Name Description MIMEType Size Downloads

Title Exploring the use of the tripeptide Gly–Gly–His as a selective recognition element for the fabrication of electrochemical copper sensors
Author(s) Yang, WenrongORCID iD for Yang, Wenrong orcid.org/0000-0001-8815-1951
Chow, Edith
Willett, Gary D.
Hibbert, D. Brynn
Gooding, J. Justin
Journal name Analyst
Volume number 128
Issue number 6
Start page 712
End page 718
Publisher Royal Society of Chemistry
Place of publication London, England
Publication date 2003
ISSN 0003-2654
1364-5528
Summary The modification of electrodes with the tripeptide Gly–Gly–His for the detection of copper in water samples is described in detail. The tripeptide modified electrode was prepared by first self-assembling 3-mercaptopropionic acid (MPA) onto the gold electrode followed by covalent attachment of the tripeptide to the self-assembled monolayer using carbodiimide coupling. The electrodes were characterized using electrochemistry, a newly developed mass-spectrometry method and quantum mechanical calculations. The mass spectrometry confirmed the modification to proceed as expected with peptide bonds formed between the carboxylic acids of the MPA and the terminal amine of the peptide. Electrochemical measurements indicated that approximately half the MPA molecules in a SAM are modified with the peptide. The peptide modified electrodes exhibited high sensitivity to copper which is attributed to the stable 4N coordinate complex the peptide formed around the metal ion to give copper the preferred tetragonal coordination. The formation of a 4 coordinate complex was predicted using quantum mechanical calculation and confirmed using mass spectrometry. The adsorption of the copper to the peptide modified electrode was consistent with a Langmuir isotherm with a binding constant of (8.1 ± 0.4) 1010 M−1 at 25 °C.
Language eng
DOI 10.1039/B212881K
Field of Research 100703 Nanobiotechnology
Socio Economic Objective 970103 Expanding Knowledge in the Chemical Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2003, The Royal Society of Chemistry
Persistent URL http://hdl.handle.net/10536/DRO/DU:30034980

Document type: Journal Article
Collection: Institute for Technology Research and Innovation
Connect to link resolver
 
Unless expressly stated otherwise, the copyright for items in DRO is owned by the author, with all rights reserved.

Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 99 times in TR Web of Science
Scopus Citation Count Cited 0 times in Scopus
Google Scholar Search Google Scholar
Access Statistics: 245 Abstract Views, 0 File Downloads  -  Detailed Statistics
Created: Mon, 30 May 2011, 10:55:40 EST

Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.