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The homogenate was further incubated for 10 min on ice in the presence of 10 mM MgCl2 and 50 μg/ml DNAse. The enlarged cell suspension was lysed using a French press with 3 passages at 500 pounds per square inch (psi). The cell lysate was centrifuged at 1,200 x g for 10 min at 4◦C to remove unbroken cells and nucleus fraction. The supernatant was collected and centrifuged at 5,000 x g for 10 min at 4◦C to remove the mitochondrial fraction and the supernatant was ultracentrifuged at 110,000 x g for 45 min at 4◦C in a Beckman TLA110 rotor. The pellet was resuspended in 200 μL of TSG buffer (50 mM Tris, pH 7.9, 100 mM NaCl, 10% glycerol) to obtain a membrane fraction called “crude membrane” and stored at -80oC until use.Crude membranes (∼1 mg) were resuspended in ice-cold TS buffer supplemented with 1% (w/v) DDM for 30 min at 4◦C with gentle shaking. The detergent extract was clarified by ultracentrifugation (110,000 x g for 15 min at 4◦C) and 1 mg aliquots (500 μl) were incubated with a 3-fold excess of His6-tagged Peptidiscs for 15 min at 4◦C. The sample was rapidly diluted to 5 mL in the TS buffer placed in a 100 kDa cutoff centrifugal filter. The sample was concentrated at 3,000 x g, 10 minutes to approximately 200 μl and diluted again to 5 ml, followed by another concentration step to approximately 200 μl. The reconstituted start Peptidisc library (4 mg total in 1 mL) was incubated with 60 μL of Ni-NTA chelating Sepharose for 1 hour at 4◦C with shaking. Following five thorough washes with TS buffer 1 mL each, the Peptidisc library was eluted in 150 μL of TS buffer containing 600 mM imidazole, recovering 1 mg at a concentration of ∼6.5 μg/μL. All fractions from the reconstitution through the purification steps were subjected to analysis by 15% SDS PAGE, followed by Coomassie blue staining of the gel. An aliquot of the purified MP library containing (∼100 μg; ∼16 μL) was treated with 6 M urea at room temperature for 30 min, followed by reduction with 10 mM DTT for 1 hour. Alkylation was performed with 20 mM IAA in the dark at room temperature for 30 min, followed by re-addition of 10 mM DTT for 30 min. The urea concentration was diluted to 1 M with 50 mM ammonium bicarbonate, pH 8.0 and trypsin was added at an enzyme/protein ratio of 1:100 for 24 h at 25°C on a shaker. Subsequently, the digested peptides were acidified to pH 3 with the addition of ∼20μl 10% formic acid and desalted using hand-packed Stage-Tips C18. The eluted peptides were dried by vacuum centrifugation.NanoLC connected to an Orbitrap Exploris mass spectrometer (Thermo Fisher Scientific) was used for the analysis of all samples. The peptide separation was carried out using a Proxeon EASY nLC 1200 System (Thermo Fisher Scientific) fitted with a custom-made C18 column (15 cm x 150 μm ID) packed with HxSil C18 3 μm Resin 100 Å (Hamilton). A gradient of water/acetonitrile/0.1% formic acid was employed for chromatography. The samples were injected onto the column and run for 180 minutes at a flow rate of 0.60 μl/min. The peptide separation began with 1% acetonitrile, increasing to 3% in the first 4 minutes, followed by a linear gradient from 3% to 23% acetonitrile over 86 minutes, then another increase from 24% to 80% acetonitrile over 35 minutes, and finally a 35-minute wash at 80% acetonitrile, and then decreasing to 1% acetonitrile for 10 min and kept 1% acetonitrile for another 10 min. The eluted peptides were ionized using positive nanoelectrospray ionization (NSI) and directly introduced into the mass spectrometer with an ion source temperature set at 250°C and an ion spray voltage of 2.1 kV. Full-scan MS spectra (m/z 350–2000) were captured in Orbitrap Exploris at a resolution of 120,000 (m/z 400). The automatic gain control was set to 1e6 for full FTMS scans and 5e4 for MS/MS scans. Ions with intensities above 1500 counts underwent fragmentation via NSI in the linear ion trap. The top 15 most intense ions with charge states of ≥2 were sequentially isolated and fragmented using normalized collision energy of 30%, activation Q of 0.250, and an activation time of 10 ms. Ions selected for MS/MS were excluded from further selection for 3 seconds. The Orbitrap Exploris mass spectrometer was operated using Thermo XCalibur software."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Data were processed using DIA-NN version 1.9.1 in library-free mode with contaminants enabled. FASTA digest–based library generation was performed with deep learning–based prediction of spectra, retention times (RTs), and ion mobilities (IMs) using the Mus musculus reference proteome (UniProt proteome ID: UP000000589). Trypsin/P was specified as the protease, allowing a maximum of one missed cleavage. No variable modifications were permitted, while N-terminal methionine excision and cysteine carbamidomethylation were enabled. The peptide length range was set to 7–30 amino acids, with a precursor charge range of 1–4. The precursor m/z range was 300–1800, and the fragment ion m/z range was 200–1800. Quantification matrices were enabled, with precursor-level false discovery rate (FDR) controlled at 1% and the log level set to 1. Heuristic protein inference was enabled with shared spectra excluded, and protein inference was performed at the gene level. The neural network classifier was run in single-pass mode. Quantification was performed using the QuantUMS (high-precision) strategy, with RT-dependent cross-run normalization enabled. Library generation included peptide identifications, RT, and IM profiling. Speed and RAM usage were set to optimize identification and quantification performance. All MS datasets were processed together within a single DIA-NN run to ensure consistent identification, quantification, and cross-run normalization across all samples."],"omics_type":["Proteomics"],"labhead":["Ashim Bhattacharya"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Department of Biochemistry and Molecular Biology, Faculty of Medicine, University of British Columbia"],"species":["Mus Musculus (mouse)"],"submitter_mail":["ashim938@student.ubc.ca"],"publication":["42067398 Bhattacharya A, Antony F, Aoki H, Babu M, Ferguson SSG, Abd-Elrahman KS, Duong van Hoa F. Membrane Proteome Remodeling in Female APP/PS1 Mice Following M1 Muscarinic Receptor Modulation Revealed by Peptidisc-Enabled DIA-MS. J Proteome Res. 2026 25(6):3136-3148 10.1021/acs.jproteome.6c00140"],"submitter_affiliation":["University of British Columbia"],"submitter_country":["Canada"],"pubmed_abstract":["Alzheimer's disease (AD) is associated with dysregulation of membrane proteins controlling amyloid processing, synaptic signaling, and neuronal communication, yet most proteomic studies focus on soluble fractions, limiting insight into membrane-centered pathology. Here, we apply a membrane-mimetic, data-independent acquisition workflow to define disease- and drug-induced remodeling of the cortical membrane proteome in an APP mouse model of AD. Female wildtype B6C3F1/J and APP/PS1 mice were aged to 9 months, treated ± the M1 positive allosteric modulator VU0486846, and validated by enrichment of APP in cortical membranes of APP/PS1 mice. This confirmed pathological context enabled direct interrogation of membrane remodeling, revealing pronounced, genotype-specific changes characterized by selective enrichment of AD-linked membrane proteins including RyR2, PLD3, ITM2C, and CNTNAP2, alongside broader shifts in pathways related to calcium signaling, synaptic organization, and membrane trafficking. In contrast, wildtype membranes were enriched in proteins associated with axon guidance and synaptic structure, such as EPHA5 and ROBO2. M1 activation produced minimal changes in wildtype mice but selectively enhanced proteins linked to neuronal trafficking and synaptic plasticity in APP/PS1 mice, including SORCS2, PLXND1, and CADM1, indicating preferential engagement of disease-altered pathways. These findings demonstrate that AD-associated remodeling is concentrated at the membrane level and highlight Peptidisc-enabled membrane proteomics as a powerful approach to resolve disease mechanisms and therapeutic target engagement."],"pubmed_title":["Membrane Proteome Remodeling in Female APP/PS1 Mice Following M1 Muscarinic Receptor Modulation Revealed by Peptidisc-Enabled DIA-MS."],"pubmed_authors":["Bhattacharya Ashim A, Antony Frank F, Aoki Hiroyuki H, Babu Mohan M, Ferguson Stephen S G SSG, Abd-Elrahman Khaled S KS, Duong van Hoa Franck F"],"additional_accession":[]},"is_claimable":false,"name":"Membrane Proteome Remodeling in Female APP Mice Following Muscarinic Acetylcholine Receptor M1 Modulation Revealed by Peptidisc Enabled DIA-MS","description":"Alzheimer’s disease (AD) is linked to profound dysregulation of membrane-embedded and membrane-associated proteins that govern amyloid processing, synaptic signaling, and neuronal communication. Yet most proteomic analyses prioritize soluble fractions, resulting in systematic underrepresentation of integral membrane proteins and limited access to disease-relevant membrane pathways. Here, we use a membrane-mimetic, data-independent acquisition proteomic workflow to define disease- and drug-induced remodeling of the cortical membrane proteome in an APP mouse model of Alzheimer’s disease. Female B6C3F1/J mice were aged to 9 months and treated for 8 weeks with or without the M1 muscarinic acetylcholine receptor positive allosteric modulator VU0486846. APP pathology drove a pronounced, genotype-specific remodeling of the membrane proteome, with enrichment of multiple membrane proteins linked to AD, including RyR2, PLD3, ITM2C, and CNTNAP2. In contrast, wild-type mice cortical membranes were enriched for membrane proteins involved in axon guidance and synaptic organization, such as EPHA5 and ROBO2. Activation of M1 using the VU0486846 produced minimal membrane proteome changes in wild-type mice but selectively enriched proteins involved in neuronal trafficking and synaptic plasticity in APP mice, including SORCS2, PLXND1, and CADM1. Together, these findings demonstrate that AD-associated proteomic remodeling is strongly concentrated at the membrane level and that M1 receptor activation preferentially engages disease-altered membrane networks rather than inducing widespread proteomic changes. This work establishes peptidisc-enabled membrane proteomics as a powerful approach for identifying membrane-associated biomarkers and evaluating therapeutic target engagement in AD.","dates":{"publication":"2026-07-10","submission":"2026-02-05"},"accession":"PXD074065","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:2042546","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:661410","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:3767","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:44250","NEWT:317447","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:12637","NEWT:2164133","NEWT:2767846","NEWT:314344","NEWT:108061","NEWT:224308","NEWT:49928","NEWT:160621","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:1310165","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1310173","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:284812","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:215451","NEWT:460519","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2709072","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:987059","NEWT:491","NEWT:460523","NEWT:85694","NEWT:85692","NEWT:3750","NEWT:291146","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:445","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:219798","NEWT:548","NEWT:150475","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:8673","NEWT:550","NEWT:10804","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:595495","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:52641","NEWT:353152","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:13037","NEWT:519","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:300641","NEWT:39655","NEWT:38323","NEWT:206411","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:510516","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:287889","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:315750","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:1436183","NEWT:4232","NEWT:9922","NEWT:416348","NEWT:11298","NEWT:4236","NEWT:398031","NEWT:196627","NEWT:523840","NEWT:1076878","NEWT:200308","NEWT:200302","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:2666255","NEWT:999810","NEWT:28995","NEWT:1392998","NEWT:1150621","NEWT:1085791","NEWT:745531","NEWT:226900","NEWT:231490","NEWT:590651","NEWT:449239","NEWT:244704","NEWT:9909","NEWT:9902","NEWT:430615","NEWT:563041","NEWT:36599","NEWT:41949","NEWT:326423","NEWT:326424","NEWT:13013","NEWT:749906","NEWT:418985","NEWT:749907","NEWT:431947","NEWT:142809","NEWT:1095183","NEWT:302409","NEWT:130821","NEWT:2320211","NEWT:27606","NEWT:290610","NEWT:1519788","NEWT:59202","NEWT:9975","NEWT:8643","NEWT:1801631","NEWT:1159899","NEWT:502780","NEWT:860688","NEWT:35231","NEWT:1774208","NEWT:8644","NEWT:1125630","NEWT:28930","NEWT:202914","NEWT:27602","NEWT:502779","NEWT:297246","NEWT:483139","NEWT:101491","NEWT:8639","NEWT:8637","NEWT:1114970","NEWT:285272","NEWT:192222","NEWT:9963","NEWT:197911",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