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|Title:||Electrochemistry of ferrocenoyl β-peptide monolayers on gold|
|Other Titles:||Electrochemistry of ferrocenoyl beta-peptide monolayers on gold|
|Citation:||Langmuir, 2010; 26(2):1334-1339|
|Publisher:||Amer Chemical Soc|
|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|
|Appears in Collections:||Chemistry publications|
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