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  • Title: Fabrication of Langmuir-Blodgett film of a fullerene derivative with a cyclic peptide as an anchor.
    Author: Fujii S, Morita T, Kimura S.
    Journal: Bioconjug Chem; 2007; 18(6):1855-9. PubMed ID: 17941685.
    Abstract:
    A novel cyclic octapeptide carrying a fullerene unit and poly(ethylene glycol) at the side chain (cyclo8-C 60 + PEG) was synthesized, and its monolayer formation at the air/water interface and on a substrate was studied. Surface pressure-area per molecule isotherms indicated that cyclo8-C 60 + PEG formed a stable monolayer at the air/water interface. The cyclo8-C 60 + PEG monolayers prepared from various spreading volumes (i.e., from various initial areas per molecule) overlapped nicely on a single curve, suggesting that the molecules were uniformly dispersed on the surface without aggregation of the fullerene units. The uniform dispersibility is due to the scaffold effect of the cyclic peptide unit to keep the fullerene units away from each other. The formed monolayer could be quantitatively transferred onto a solid substrate. UV-vis absorption spectroscopy of the Langmuir-Blodgett (LB) monolayer showed that the electronic structure of the fullerene unit was not affected by the formation of the monolayer. Cyclic voltammetry of the LB monolayer in an aqueous solution containing redox species indicated that the LB monolayer was densely packed. Furthermore, reversible redox peaks attributed to the one-electron reduction of the fullerene unit were observed, showing that the redox property of the fullerene unit was also retained in the monolayer. It is thus concluded that the cyclic peptide is a good candidate as a scaffold for stable monolayer formation at the air/water interface and for intact immobilization of the fullerene moiety onto a substrate.
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