Orthogonal (19) F-Labeling for Solid-State NMR Spectroscopy Reveals the Conformation and Orientation of Short Peptaibols in Membranes(67 visite) Grage SL, Kara S, Bordessa A, Doan V, Rizzolo F, Putzu M, Kubar T, Papini AM, Chaume G, Brigaud T, Afonin S, Ulrich AS
Chemistry (ISSN: 1521-3765electronic, 0947-6539linking), 2018 Jan 11; N/D: N/D-N/D.
Tipo di articolo: Journal Article,
Impact factor: 5.476, Impact factor a 5 anni: 5.477
Url: Non disponibile.
Parole chiave: Nmr Spectroscopy, Amino Acids, Fluorine, Isotopic Labeling, Peptides,
Affiliazioni:
*** IBB - CNR *** Institute of Biological Interfaces (IBG-2), Karlsruhe Institute of Technology (KIT), POB 3640, 76021, Karlsruhe, Germany., Institute of Organic Chemistry (IOC), KIT, Fritz-Haber Weg 6, 76131, Karlsruhe, Germany., Laboratoire de Chimie Biologique (LCB), EA4505, Platform PeptLab@UCP, Universite de Cergy-Pontoise, 5 Mail Gay-Lussac, Neuville sur Oise, 95000, Cergy-Pontoise cedex, France., French-Italian Interdepartmental Laboratory of Peptide and Protein Chemistry and Biology (PeptLab), Department of Chemistry "Ugo Schiff", CNR-IBB, University of Florence, 50019, Sesto Fiorentino, Italy., Institute of Physical Chemistry (IPC), Center for Functional Nanostructures (CFN), KIT, 76131, Karlsruhe, Germany.,
Riferimenti:
Non disponibile.
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, (R)- and (S)-trifluoromethylalanine, and (15) N-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 (19) F and (15) N NMR spectroscopy. This strategy revealed a beta-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.
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