Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/61718
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Type: Journal article
Title: Electrochemistry of ferrocenoyl β-peptide monolayers on gold
Other Titles: Electrochemistry of ferrocenoyl beta-peptide monolayers on gold
Author: Brooksby, P.
Anderson, K.
Downard, A.
Abell, A.
Citation: Langmuir, 2010; 26(2):1334-1339
Publisher: Amer Chemical Soc
Issue Date: 2010
ISSN: 0743-7463
1520-5827
Statement of
Responsibility: 
Paula A. Brooksby, Kelly H. Anderson, Alison J. Downard and Andrew D. Abell
Abstract: The electrochemistry of self-assembled monolayers (SAMs) on gold containing a lipoic acid linker, the beta-peptide sequence (beta(3)Val-beta(3)Ala-beta(3)Leu)(n) for n = 1, 2, and a terminal ferrocenyl group has been described for the first time. Circular dichroism (CD), NMR, and molecular modeling were used to evaluate the beta-peptide structure in solution, while the monolayer film organization and electron-transfer kinetics were evaluated by cyclic voltammetry, chronoamperometry (CA), and ellipsometry. The peptides were assembled from trifluoroethanol solutions, where they are linear (n = 1) or helical (n = 2) based on CD, NMR, ellipsometry, and modeling evidence. The structure of the SAMs is less well understood. There is evidence for noncompact layers that allow electrolyte ions to approach the interface. Electron-transfer rates for n = 1, 2 were found to be 2500 and 1200 s(-1), respectively, and CA evidence indicated that the transfer is based on the hopping mechanism.
Keywords: Gold; Trifluoroethanol; Peptides; Circular Dichroism; Magnetic Resonance Spectroscopy; Molecular Structure; Electrochemistry
Rights: Copyright © 2010 American Chemical Society
RMID: 0020100098
DOI: 10.1021/la902402t
Appears in Collections:Chemistry publications

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