A generalized approach for NMR studies of lipid-protein interactions based on sparse fluorination of acyl chains.
journal contribution
posted on 2018-08-31, 08:50 authored by Alfredo De Biasio, Alain Ibáñez de Opakua, Mark J. Bostock, Daniel Nietlispach, Tammo Diercks, Francisco J. BlancoSparse lipid fluorination enhances the lipids' 1H signal dispersion, enables clean molecular distinction by 19F NMR, and evinces micelle insertion of proteins via fluorine-induced signal shifts. We present a minimal fluorination scheme, and illustrate the concept on di-(4-fluoro)-heptanoylphosphatidylcholine micelles and solubilised seven-helix transmembrane pSRII protein.
Funding
We thank MINECO for the Severo Ochoa Excellence Accreditation (SEV-2016-0644) and for the grant CTQ2017-83810-R to FJB.
History
Citation
Chemical Communications, 2018, 54 (53), pp. 7306-7309Author affiliation
/Organisation/COLLEGE OF LIFE SCIENCES/Biological Sciences/Molecular & Cell BiologyVersion
- VoR (Version of Record)
Published in
Chemical CommunicationsPublisher
Royal Society of Chemistryissn
1359-7345eissn
1364-548XAcceptance date
2018-05-21Copyright date
2018Available date
2018-08-31Publisher DOI
Publisher version
http://pubs.rsc.org/en/Content/ArticleLanding/2018/CC/C8CC02483A#!divAbstractNotes
Electronic supplementary information (ESI) available: Experimental procedures, figures and tables. See DOI: 10.1039/c8cc02483aLanguage
enAdministrator link
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