Quenching of the excited states of a chromophore by a suitable moiety can provide important information on the probe-quencher distance. Singlet quenching through Förster energy transfer has been exploited by us in the determination of the structural features of many ordered oligopeptides in solution, by combining experimental data with molecular modeling studies. Quenching of excited triplet states would extend this approach from the nanoseconds time-region of singlet lifetimes to the microseconds, possibly providing new insights on peptide dynamics. To verify the scope of this method, we have investigated the distance dependence of the intramolecular quenching of the benzophenone triplet of the Bpa residue by the nitroxide radical of TOAC in the oligopeptides listed in Figure 1. BT0 Boc-Aib-Bpa-TOAC-Ala-Aib-Aib-Ala-OtBu BT1 Boc-Aib-Bpa-Aib-TOAC-Ala-Aib-Ala-OtBu BT2 Boc-Aib-Bpa-Aib-Ala-TOAC-Aib-Ala-OtBu BT3 Boc-Aib-Bpa-Aib-Aib-Ala-TOAC-Ala-OtBu B Boc-Bpa-Aib-Aib-Aib-Aib-Aib-OtBu
Stella, L., Bocchinfuso, G., Gatto, E., Palleschi, A., Venanzi, M., Zavallone, D., et al. (2006). Intramolecular Triplet Quenching by Nitroxide Radicals as a Tool for Determining Peptide Secondary Structure in Solution.. In S.E. Blondelle (a cura di), Understanding Biology Using Peptides (pp. 603-604). American Peptide Society.
Intramolecular Triplet Quenching by Nitroxide Radicals as a Tool for Determining Peptide Secondary Structure in Solution.
STELLA, LORENZO;BOCCHINFUSO, GIANFRANCO;GATTO, EMANUELA;PALLESCHI, ANTONIO;VENANZI, MARIANO;PISPISA, BASILIO
2006-01-01
Abstract
Quenching of the excited states of a chromophore by a suitable moiety can provide important information on the probe-quencher distance. Singlet quenching through Förster energy transfer has been exploited by us in the determination of the structural features of many ordered oligopeptides in solution, by combining experimental data with molecular modeling studies. Quenching of excited triplet states would extend this approach from the nanoseconds time-region of singlet lifetimes to the microseconds, possibly providing new insights on peptide dynamics. To verify the scope of this method, we have investigated the distance dependence of the intramolecular quenching of the benzophenone triplet of the Bpa residue by the nitroxide radical of TOAC in the oligopeptides listed in Figure 1. BT0 Boc-Aib-Bpa-TOAC-Ala-Aib-Aib-Ala-OtBu BT1 Boc-Aib-Bpa-Aib-TOAC-Ala-Aib-Ala-OtBu BT2 Boc-Aib-Bpa-Aib-Ala-TOAC-Aib-Ala-OtBu BT3 Boc-Aib-Bpa-Aib-Aib-Ala-TOAC-Ala-OtBu B Boc-Bpa-Aib-Aib-Aib-Aib-Aib-OtBuI documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
