AI Article Synopsis
- - The study investigates the suitability of diazirine-modified lipids, specifically DiazPC, for studying lipid/peptide interactions using cross-linking mass spectrometry (XL-MS).
- - Researchers found that the diazirine group's stearoyl chain exhibited unexpected backfolding behavior in membranes with the α-helical peptide LAVA20.
- - This behavior raises concerns about the effectiveness of DiazPC for future XL-MS studies and suggests that such behavior may apply to other modified lipids, impacting future research on protein/lipid interactions.
Article Abstract
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.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8597076 | PMC |
| http://dx.doi.org/10.1002/chem.202102048 | DOI Listing |
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