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- Title
Orthogonal <sup>19</sup>F‐Labeling for Solid‐State NMR Spectroscopy Reveals the Conformation and Orientation of Short Peptaibols in Membranes.
- Authors
Grage, Stephan L.; Kara, Sezgin; Bordessa, Andrea; Doan, Véronique; Rizzolo, Fabio; Putzu, Marina; Kubař, Tomáš; Papini, Anna Maria; Chaume, Grégory; Brigaud, Thierry; Afonin, Sergii; Ulrich, Anne S.
- Abstract
Abstract: Peptaibols are promising drug candidates in view of their interference with cellular membranes. Knowledge of their lipid interactions and membrane‐bound structure is needed to understand their activity and should be, in principle, accessible by solid‐state NMR spectroscopy. However, their unusual amino acid composition and noncanonical conformations make it very challenging to find suitable labels for NMR spectroscopy. Particularly in the case of short sequences, new strategies are required to maximize the structural information that can be obtained from each label. Herein, l‐3‐(trifluoromethyl)bicyclopent[1.1.1]‐1‐ylglycine, (<italic>R</italic>)‐ and (<italic>S</italic>)‐trifluoromethylalanine, and 15N‐backbone labels, each probing a different direction in the molecule, have been combined to elucidate the conformation and membrane alignment of harzianin HK‐VI. For the short sequence of 11 amino acids, 12 orientational constraints have been obtained by using 19F and 15N NMR spectroscopy. This strategy revealed a β‐bend ribbon structure, which becomes realigned in the membrane from a surface‐parallel state towards a membrane‐spanning state, with increasing positive spontaneous curvature of the lipids.
- Subjects
ORGANIC solid state chemistry; NUCLEAR magnetic resonance spectroscopy; AMINO acids; AMINO compounds; ARTIFICIAL membranes
- Publication
Chemistry - A European Journal, 2018, Vol 24, Issue 17, p4328
- ISSN
0947-6539
- Publication type
Article
- DOI
10.1002/chem.201704307