%0 Artikel






%@ 0947-6539
%A Dorner, J.
%A  Korn, P.
%A  Gruhle, K.
%A  Ramsbeck, D.
%A  Garamus, V.
%A  Lilie, H.
%A  Meister, A.
%A  Schwieger, C.
%A  Ihling, C.
%A  Sinz, A.
%A  Drescher, S.

%D 2021
%J Chemistry - A European Journal
%N 1682
%P 14586 - 14593 
%R doi:10.1002/chem.202102048
%T A Diazirine-Modified Membrane Lipid to Study Peptide/Lipid Interactions – Chances and Challenges
%U https://dx.doi.org/10.1002/chem.202102048
59 
%X 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 behavior 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 behavior 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.