Peptide foldamers based on alpha,alpha-disubstituted glycyl residues were synthesized and chemically characterized to investigate the effects of the electric field generated by a 3(10)-helix on the rate of intramolecular photoinduced electron-transfer reactions. To this end, two new octapeptides having identical sequences were suitably side-chain functionalized with the same electron-transfer donor-acceptor pair, but inverting the position of the pair along the main chain. The electron-transfer rate constants, measured by time-resolved spectroscopy techniques (nanosecond transient absorption and time-resolved fluorescence), indicated that, in the case of the 3(10)-helix, the electrostatic effect is significant, but smaller than that obtained for alpha-helical peptides. This finding can be likely ascribed to the distortion of the H-bond network with respect to the helical axis taking place in the former secondary structure. Overall, these results could have implications on electron-transfer phenomena in model and biomembranes facilitated by peptaibiotics.

Gatto, E., Porchetta, A., Stella, L., Guryanov, I., Formaggio, F., Toniolo, C., et al. (2008). Conformational effects on the electron-transfer efficiency in peptide foldamers based on alpha,alpha-disubstituted glycyl residues. CHEMISTRY & BIODIVERSITY, 5(7), 1263-1278 [10.1002/cbdv.200890113].

Conformational effects on the electron-transfer efficiency in peptide foldamers based on alpha,alpha-disubstituted glycyl residues

GATTO, EMANUELA;Porchetta, A;STELLA, LORENZO;VENANZI, MARIANO
2008-07-01

Abstract

Peptide foldamers based on alpha,alpha-disubstituted glycyl residues were synthesized and chemically characterized to investigate the effects of the electric field generated by a 3(10)-helix on the rate of intramolecular photoinduced electron-transfer reactions. To this end, two new octapeptides having identical sequences were suitably side-chain functionalized with the same electron-transfer donor-acceptor pair, but inverting the position of the pair along the main chain. The electron-transfer rate constants, measured by time-resolved spectroscopy techniques (nanosecond transient absorption and time-resolved fluorescence), indicated that, in the case of the 3(10)-helix, the electrostatic effect is significant, but smaller than that obtained for alpha-helical peptides. This finding can be likely ascribed to the distortion of the H-bond network with respect to the helical axis taking place in the former secondary structure. Overall, these results could have implications on electron-transfer phenomena in model and biomembranes facilitated by peptaibiotics.
lug-2008
Pubblicato
Rilevanza nazionale
Articolo
Sì, ma tipo non specificato
Settore CHIM/02 - CHIMICA FISICA
English
Con Impact Factor ISI
Static Electricity; Aminoisobutyric Acids; Protein Structure, Secondary; Spectrometry, Fluorescence; Electron Transport; Glycine; Spectrophotometry, Ultraviolet; Peptaibols; Oligopeptides; Hydrogen Bonding; Valine
Gatto, E., Porchetta, A., Stella, L., Guryanov, I., Formaggio, F., Toniolo, C., et al. (2008). Conformational effects on the electron-transfer efficiency in peptide foldamers based on alpha,alpha-disubstituted glycyl residues. CHEMISTRY & BIODIVERSITY, 5(7), 1263-1278 [10.1002/cbdv.200890113].
Gatto, E; Porchetta, A; Stella, L; Guryanov, I; Formaggio, F; Toniolo, C; Kaptein, B; Broxterman, Q; Venanzi, M
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/27721
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