10.1021/ja072851d.s001
Alexander D. Milov
Alexander D.
Milov
Rimma I. Samoilova
Rimma I.
Samoilova
Yuri D. Tsvetkov
Yuri D.
Tsvetkov
Fernando Formaggio
Fernando
Formaggio
Claudio Toniolo
Claudio
Toniolo
Jan Raap
Jan
Raap
Self-Aggregation of Spin-Labeled Alamethicin in ePC Vesicles Studied by
Pulsed Electron−Electron Double Resonance
American Chemical Society
2007
position 16
resonance technique
0.2.
3.5
acid
concentration
2.3 nm
label
width
Electron
function
model
peptide
ePC Vesicles Studied
77 K
electron
interaction
1.3 nm
ePC vesicles
tetramethylpiperidine
form aggregates
Pulsed
ResonanceThe
4.2
Alamethicin
alamethicin molecules
data
alamethicin analogue
2007-08-01 00:00:00
Journal contribution
https://acs.figshare.com/articles/journal_contribution/Self_Aggregation_of_Spin_Labeled_Alamethicin_in_ePC_Vesicles_Studied_by_Pulsed_Electron_Electron_Double_Resonance/2993779
The pulsed electron−electron double resonance technique was used to study the dipole−dipole interactions between 2,2,6,6-tetramethylpiperidine-1-oxyl-4-amino-4-carboxylic acid spin labels located at position 16 of an alamethicin analogue in ePC vesicles that were frozen to 77 K. We show that under these conditions the alamethicin molecules tend to form aggregates over the range of peptide concentrations 3.5 × 10<sup>-3</sup> to 1 × 10<sup>-2</sup> M. The number of molecules in the aggregate is found to be 4.2 ± 0.2. A spin-label distance distribution function is also obtained with a maximum at a distance of 2.3 nm and a half-height width of 1.3 nm. We envisage that these data will permit us to generate a molecular model of cellular ion channels