English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Semi‐rigid nitroxide spin label for long‐range EPR distance measurements of lipid bilayer embedded β‐peptides.

MPS-Authors
/persons/resource/persons228234

Valora,  G.
Research Group of Electron Paramagnetic Resonance, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons136378

Halbmair,  K.
Research Group of Electron Paramagnetic Resonance, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons228236

Kehl,  A.
Research Group of Electron Paramagnetic Resonance, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons14834

Bennati,  M.
Research Group of Electron Paramagnetic Resonance, MPI for Biophysical Chemistry, Max Planck Society;

External Ressource
No external resources are shared
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)

3011488_Suppl.pdf
(Supplementary material), 3MB

Citation

Wegner, J., Valora, G., Halbmair, K., Kehl, A., Worbs, B., Bennati, M., et al. (2019). Semi‐rigid nitroxide spin label for long‐range EPR distance measurements of lipid bilayer embedded β‐peptides. Chemistry - A European Journal, 25(9), 2203-2207. doi:10.1002/chem.201805880.


Cite as: http://hdl.handle.net/21.11116/0000-0002-98BA-1
Abstract
β‐Peptides are an interesting new class of transmembrane model peptides based on their conformationally stable and well‐defined secondary structures. Herein, we present the synthesis of the paramagnetic β‐amino acid β3‐hTOPP (4‐(3,3,5,5‐tetramethyl‐2,6‐dioxo‐4‐oxylpiperazin‐1‐yl)‐d‐β3‐homophenylglycine) that enables investigations of β‐peptides by EPR spectroscopy. This amino acid adds to the so far sparse number of β‐peptide spin labels. Its performance was evaluated by investigating the helical turn of a 314‐helical transmembrane model β‐peptide. Nanometer distances between two incorporated β3‐hTOPP labels in different environments were measured using PELDOR/DEER (pulsed electron‐electron double resonance) spectroscopy. Due to the semi‐rigid conformational design, the label delivers reliable distances and sharp (one‐peak) distance distributions even in the lipid bilayer. The results indicate that the investigated β‐peptide folds into a 3.2514 helix and maintains this conformation in the lipid bilayer.