Cation recognition by self-assembled monolayers of oriented helical peptides having a crown ether unit.
Cation recognition of self-assembled monolayers (SAMs) of helical peptides having a crown ether unit was investigated by the impedance spectroscopy and cyclic voltammetry. Lipo-(Ala-Aib)8-Ala-Cr and Boc-Glu(Cr)-(Ala-Aib)8-Lipoa (Lipo, Lipoa, and Cr represent lipoic acid, lipoamide, and amidobenzo-18-crown-6, respectively) were synthesized and the helix SAMs were prepared. The peptides having a crown ether unit formed SAMs oriented nearly vertically to the substrate. The capacitance of the Lipo-(Ala-Aib)(8)-Ala-Cr SAM changed specifically with the addition of cations, and the binding constants of the SAM were larger than those of the crown ether in aqueous solution because of a large dipole moment of the helical peptide. In the case of the Boc-Glu(Cr)-(Ala-Aib)8-Lipoa SAM, the cation binding to the SAM showed a drastic decrease in the peak current of the cyclic voltammetry around 10(-5)M of K+ ion. In either capacitance measurement or cyclic voltammetry, the helical peptide SAM played an important role in the sensitive response to cations.
Miura
Y
Y
Department of Material Chemistry, Graduate School of Engineering, Kyoto University, Yoshida Honmachi Sakyoku, Kyoto 606-8501, Japan.
Kimura
S
S
Kobayashi
S
S
Imanishi
Y
Y
Umemura
J
J
D002412:Cations / Q000378:metabolism*; D017097:Electric Impedance; D004563:Electrochemistry; D004988:Ethers, Cyclic / Q000737:chemistry* / Q000378:metabolism; D005782:Gels; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D011188:Potassium / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared; D013379:Substrate Specificity
D002412:Cations; D004988:Ethers, Cyclic; D005782:Gels; D010455:Peptides; D011188:Potassium