Electrochemistry of Ferrocenoyl β-Peptide Monolayers on Gold
journal contributionposted on 19.01.2010, 00:00 by Paula A. Brooksby, Kelly H. Anderson, Alison J. Downard, Andrew D. Abell
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The electrochemistry of self-assembled monolayers (SAMs) on gold containing a lipoic acid linker, the β-peptide sequence (β3Val-β3Ala-β3Leu)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 β-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.