Language
English
Publication Date
8-16-2023
Journal
Chemical Science
DOI
10.1039/d3sc01482g
PMID
37593000
PMCID
PMC10430552
PubMedCentral® Posted Date
7-21-2023
PubMedCentral® Full Text Version
Post-print
Abstract
While it is known that lipids play an essential role in regulating membrane protein structure and function, it remains challenging to identify specific protein-lipid interactions. Here, we present an innovative approach that combines native mass spectrometry (MS) and lipidomics to identify lipids retained by membrane proteins from natural lipid extracts. Our results reveal that the bacterial ammonia channel (AmtB) enriches specific cardiolipin (CDL) and phosphatidylethanolamine (PE) from natural headgroup extracts. When the two extracts are mixed, AmtB retains more species, wherein selectivity is tuned to bias headgroup selection. Using a series of natural headgroup extracts, we show TRAAK, a two-pore domain K
Published Open-Access
yes
Recommended Citation
Zhu, Yun; Odenkirk, Melanie T; Qiao, Pei; et al., "Combining Native Mass Spectrometry and Lipidomics To Uncover Specific Membrane Protein-Lipid Interactions From Natural Lipid Sources" (2023). Faculty and Staff Publications. 3871.
https://digitalcommons.library.tmc.edu/baylor_docs/3871