Backbone Dynamics of Alamethicin Bound to Lipid Membranes: Spin-Echo Electron Paramagnetic Resonance of TOAC-Spin Labels Export

@article{citeulike:2522953, abstract = {Alamethicin F50/5 is a hydrophobic peptide that is devoid of charged residues and that induces voltage-dependent ion channels in lipid membranes. The peptide backbone is likely to be involved in the ion conduction pathway. Electron spin-echo spectroscopy of alamethicin F50/5 analogs in which a selected Aib residue (at position n = 1, 8, or 16) is replaced by the TOAC amino-acid spin label was used to study torsional dynamics of the peptide backbone in association with phosphatidylcholine bilayer membranes. Rapid librational motions of limited angular amplitude were observed at each of the three TOAC sites by recording echo-detected spectra as a function of echo delay time, 2{tau}. Simulation of the time-resolved spectra, combined with conventional EPR measurements of the librational amplitude, shows that torsional fluctuations of the peptide backbone take place on the subnanosecond to nanosecond timescale, with little temperature dependence. Associated fluctuations in polar fields from the peptide could facilitate ion permeation. 10.1529/biophysj.107.115287}, author = {Bartucci, Rosa and Guzzi, Rita and De Zotti, Marta and Toniolo, Claudio and Sportelli, Luigi and Marsh, Derek}, citeulike-article-id = {2522953}, citeulike-linkout-0 = {http://dx.doi.org/10.1529/biophysj.107.115287}, citeulike-linkout-1 = {http://www.biophysj.org/cgi/content/abstract/94/7/2698}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/18096632}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=18096632}, day = {1}, doi = {10.1529/biophysj.107.115287}, journal = {Biophys. J.}, keywords = {alamethicin, dynamics, experimental, membrane, peptide}, month = {April}, number = {7}, pages = {2698--2705}, posted-at = {2008-03-12 22:52:12}, priority = {2}, title = {Backbone Dynamics of Alamethicin Bound to Lipid Membranes: Spin-Echo Electron Paramagnetic Resonance of TOAC-Spin Labels}, url = {http://dx.doi.org/10.1529/biophysj.107.115287}, volume = {94}, year = {2008} }

TY - JOUR ID - citeulike:2522953 L3 - citeulike-article-id:2522953 N2 - Alamethicin F50/5 is a hydrophobic peptide that is devoid of charged residues and that induces voltage-dependent ion channels in lipid membranes. The peptide backbone is likely to be involved in the ion conduction pathway. Electron spin-echo spectroscopy of alamethicin F50/5 analogs in which a selected Aib residue (at position n = 1, 8, or 16) is replaced by the TOAC amino-acid spin label was used to study torsional dynamics of the peptide backbone in association with phosphatidylcholine bilayer membranes. Rapid librational motions of limited angular amplitude were observed at each of the three TOAC sites by recording echo-detected spectra as a function of echo delay time, 2{tau}. Simulation of the time-resolved spectra, combined with conventional EPR measurements of the librational amplitude, shows that torsional fluctuations of the peptide backbone take place on the subnanosecond to nanosecond timescale, with little temperature dependence. Associated fluctuations in polar fields from the peptide could facilitate ion permeation. 10.1529/biophysj.107.115287 IS - 7 JF - Biophys. J. EP - 2705 TI - Backbone Dynamics of Alamethicin Bound to Lipid Membranes: Spin-Echo Electron Paramagnetic Resonance of TOAC-Spin Labels VL - 94 SP - 2698 KW - alamethicin KW - dynamics KW - experimental KW - membrane KW - peptide AU - Bartucci, Rosa AU - Guzzi, Rita AU - De Zotti, Marta AU - Toniolo, Claudio AU - Sportelli, Luigi AU - Marsh, Derek PY - 2008/04/01/ UR - http://dx.doi.org/10.1529/biophysj.107.115287 ER -