Identifying Membrane Protein-Lipid Interactions with Lipidomic Lipid Exchange-Mass Spectrometry.
Journal
Journal of the American Chemical Society
ISSN: 1520-5126
Titre abrégé: J Am Chem Soc
Pays: United States
ID NLM: 7503056
Informations de publication
Date de publication:
27 09 2023
27 09 2023
Historique:
pmc-release:
27
09
2024
medline:
28
9
2023
pubmed:
13
9
2023
entrez:
13
9
2023
Statut:
ppublish
Résumé
Lipids can play important roles in modulating membrane protein structure and function. However, it is challenging to identify natural lipids bound to membrane proteins in complex bilayers. Here, we developed lipidomic lipid exchange-mass spectrometry (LX-MS) to study the lipid affinity for membrane proteins on a lipidomic scale. We first mix membrane protein nanodiscs with empty nanodiscs that have no embedded membrane proteins. After allowing lipids to passively exchange between the two populations, we separate the two types of nanodiscs and perform lipidomic analysis on each with liquid chromatography and MS. Enrichment of lipids in the membrane protein nanodiscs reveals the affinity of individual lipids for binding the target membrane protein. We apply this approach to study three membrane proteins. With the
Identifiants
pubmed: 37700579
doi: 10.1021/jacs.3c05883
pmc: PMC10540470
mid: NIHMS1931477
doi:
Substances chimiques
Membrane Lipids
0
Membrane Proteins
0
AmtB protein, E coli
0
Cation Transport Proteins
0
Escherichia coli Proteins
0
Types de publication
Journal Article
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
20859-20867Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM128624
Pays : United States
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