A generalized approach for NMR studies of lipid-protein interactions based on sparse fluorination of acyl chains

Alfredo De Biasio; Alain Ibáñez De Opakua; Mark J. Bostock; Daniel Nietlispach; Tammo Diercks; Francisco J. Blanco

doi:10.1039/c8cc02483a

A generalized approach for NMR studies of lipid-protein interactions based on sparse fluorination of acyl chains

Alfredo De Biasio, Alain Ibáñez De Opakua, Mark J. Bostock, Daniel Nietlispach, Tammo Diercks, Francisco J. Blanco

Research output: Contribution to journal › Article › peer-review

1 Scopus citations

Abstract

Sparse 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.

Original language	English (US)
Pages (from-to)	7306-7309
Number of pages	4
Journal	Chemical Communications
Volume	54
Issue number	53
DOIs	https://doi.org/10.1039/c8cc02483a
State	Published - Jan 1 2018
Externally published	Yes

Access to Document

10.1039/c8cc02483a

Cite this

@article{5ff5e34c622f4b5e8ab1725ff0aa4c74,

title = "A generalized approach for NMR studies of lipid-protein interactions based on sparse fluorination of acyl chains",

abstract = "Sparse 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.",

author = "{De Biasio}, Alfredo and {Ib{\'a}{\~n}ez De Opakua}, Alain and Bostock, {Mark J.} and Daniel Nietlispach and Tammo Diercks and Blanco, {Francisco J.}",

note = "Generated from Scopus record by KAUST IRTS on 2022-09-13",

year = "2018",

month = jan,

day = "1",

doi = "10.1039/c8cc02483a",

language = "English (US)",

volume = "54",

pages = "7306--7309",

journal = "Chemical Communications",

issn = "1364-548X",

publisher = "ROYAL SOC CHEMISTRY",

number = "53",

}

TY - JOUR

T1 - A generalized approach for NMR studies of lipid-protein interactions based on sparse fluorination of acyl chains

AU - De Biasio, Alfredo

AU - Ibáñez De Opakua, Alain

AU - Bostock, Mark J.

AU - Nietlispach, Daniel

AU - Diercks, Tammo

AU - Blanco, Francisco J.

N1 - Generated from Scopus record by KAUST IRTS on 2022-09-13

PY - 2018/1/1

Y1 - 2018/1/1

N2 - Sparse 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.

AB - Sparse 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.

UR - http://xlink.rsc.org/?DOI=C8CC02483A

UR - http://www.scopus.com/inward/record.url?scp=85049350093&partnerID=8YFLogxK

U2 - 10.1039/c8cc02483a

DO - 10.1039/c8cc02483a

M3 - Article

SN - 1364-548X

VL - 54

SP - 7306

EP - 7309

JO - Chemical Communications

JF - Chemical Communications

IS - 53

ER -

A generalized approach for NMR studies of lipid-protein interactions based on sparse fluorination of acyl chains

Abstract

Access to Document

Other files and links

Fingerprint

Cite this