biostudies-literatureDeedwania AMedical Research CouncilRoyal SocietyEngineering and Physical Sciences Research Council120-128https://www.ebi.ac.uk/biostudies/studies/S-EPMC12560048biostudies-literatureUnknown7(1)Membrane proteins and lipids are essential for a wide range of cellular processes, making their structural characterisation essential for understanding biological function. However, the amphipathic nature of membrane proteins poses a significant challenge for traditional structural biology techniques. Membrane mimetics offer an alternative approach to studying membrane proteins in more native-like environments. Among them, peptidiscs have emerged as a promising tool for stabilising membrane proteins, allowing reconstitution from detergent micelles into a detergent-free, native-like environment that preserves structural integrity. While peptidiscs have shown utility in techniques such as mass photometry and cryo-EM, their compatibility with native mass spectrometry (MS) remains largely unexRSC chemical biologyNative mass spectrometry of membrane proteins reconstituted in peptidiscs.PMC12560048MR/V028839/1URF\R1\211567EP/Y036158/1Deedwania ARobinson CVWang YBolla JRfalseNative mass spectrometry of membrane proteins reconstituted in peptidiscs.Membrane proteins and lipids are essential for a wide range of cellular processes, making their structural characterisation essential for understanding biological function. However, the amphipathic nature of membrane proteins poses a significant challenge for traditional structural biology techniques. Membrane mimetics offer an alternative approach to studying membrane proteins in more native-like environments. Among them, peptidiscs have emerged as a promising tool for stabilising membrane proteins, allowing reconstitution from detergent micelles into a detergent-free, native-like environment that preserves structural integrity. While peptidiscs have shown utility in techniques such as mass photometry and cryo-EM, their compatibility with native mass spectrometry (MS) remains largely unex2026-01-01T00:00:00Z2026 Jan2026-06-13T04:55:31.748Z2026-06-13T03:08:59.731ZS-EPMC125600484116434410.1039/d5cb00236b