Premium
A Diazirine‐Modified Membrane Lipid to Study Peptide/Lipid Interactions – Chances and Challenges
Author(s) -
Dorner Julia,
Korn Patricia,
Gruhle Kai,
Ramsbeck Daniel,
Garamus Vasil M.,
Lilie Hauke,
Meister Annette,
Schwieger Christian,
Ihling Christian,
Sinz Andrea,
Drescher Simon
Publication year - 2021
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.202102048
Subject(s) - diazirine , chemistry , peptide , lipid bilayer , moiety , membrane , alkyl , biophysics , biochemistry , stereochemistry , organic chemistry , biology
Although incorporation of photo‐activatable lipids into membranes potentially opens up novel avenues for investigating interactions with proteins, the question of whether diazirine‐modified lipids are suitable for such studies, remains under debate. Focusing on the potential for studying lipid/peptide interactions by cross‐linking mass spectrometry (XL‐MS), we developed a diazirine‐modified lipid (DiazPC), and examined its behaviour in membranes incorporating the model α‐helical peptide LAVA20. We observed an unexpected backfolding of the diazirine‐containing stearoyl chain of the lipid. This surprising behaviour challenges the potential application of DiazPC for future XL‐MS studies of peptide and protein/lipid interactions. The observations made for DiazPC most likely represent a general phenomenon for any type of membrane lipids with a polar moiety incorporated into the alkyl chain. Our finding is therefore of importance for future protein/lipid interaction studies relying on modified lipid probes.