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Edwards"],"technology_type":["Mass Spectrometry","Bottom-up proteomics","Data-independent acquisition"],"software":[""],"submitter_keywords":["Plasma proteomics","Lcms","Clinical proteomics","Astral"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD069060"],"tissue":["Blood Plasma"],"sample_protocol":["Neat plasma preparation was performed using the Universal Solid-Phase Protein Preparation (USP3) method (Dagley et al., 2019). Briefly, 2 μL of plasma was thawed at 20 °C and solubilised in 100 μL of lysis buffer (2% SDS, 100 mM Tris-HCl, pH 8.5, 10 mM TCEP, 40 mM 2-CAA). A volume of 20 μL carboxy magnetic beads (Cube Biotech) were used for on-bead capture and digestion. A total of 20 μg of lysed protein was added to beads, and then on-bead precipitation was performed at 70% v/v ACN at RT for 20 minutes with shaking at 400 rpm (ThermoMixer C, Eppendorf). After this the supernatant was removed, beads were washed twice with 200 μL of 70% ethanol, and once with 200 μL of ACN. Solvent traces were removed using a centrifugal concentrator (CentriVap, Labconco), and digestion performed in 50 μL of digestion buffer (100 mM Tris-HCl, 1:50 Lys-C, 1:50 trypsin) at 37 °C for 1 hour with shaking at 400 rpm (ThermoMixer C, Eppendorf). Afterwards digests were acidified with 5 μL of 10% formic acid (FA) and desalted using C18 stage tips (AffiniSep, France). The resultant peptides were lyophilised on centrifugal concentrator (CentriVap, Labconco) before reconstitution in 150 μL of MS-loading buffer (0.1% FA, 2% ACN) containing iRT peptides prepared according to the manufacturer's instructions (25 μL of iRT-peptide mix was diluted with 640 μL of MS loading-buffer (MS/iRT-loading buffer)). Post-digest and reconstitution, four technical replicates of PPP and PRP samples and PPP:PRP mixes were prepared. Aliquots were frozen and a fresh aliquot thawed and used fresh for each instrument as required. All LC-MS runs were acquired on one of three instruments: Orbitrap Astral MS (ThermoFisher Scientific), timsTOF Pro MS (Bruker), Orbitrap Eclipse Tribrid MS (ThermoFisher Scientific). On all instruments the plasma samples were separated on an Aurora ‘Elite’ (IonOpticks) fused silica column (i.d. 75 μm, o.d. 360 μm, 15 cm length, 1.7 μm C18 beads) with an integrated emitter tip at 50oC, using either a Vanquish Neo UHPLC (Vanquish; Thermo) for the Thermo Orbitrap instruments, or nanoflow HPLC (PAL) connected  with a Dionex UltiMate 3000 pump (Dionex; Thermo) for the timsTOFpro. Vanquish column loading was pressure-controlled (1500 bar) with a maximum flowrate of 1.5 μL/min, while Dionex column loading was performed at 600 μL/min over 9 minutes. Separation was achieved on either a 15, 22, 30, or 45-minute linear gradient, from 2% or 3.4% to 34% ACN composition.   For the Orbitrap Astral MS, three data-independent acquisition (DIA) methods were used and named A1, A2, A3. Briefly these will be referred to as method A1 (a detection-focused method with 2 Th MS2 windows and  maximum injection time (maxIT) of 7 ms (Hendricks et al., 2024)), method A2 (a quantification-focused method with 4 Th MS2 windows and a maxIT of 10 ms (Heil et al., 2023) and method A3 (an in-house HeLa-optimised method using 200 variable-width MS2 windows and a maxIT of 3 ms). As noted above, method A3 was derived from a cell lysate-optimised method, whereas methods A1 and A2 were optimised for plasma protein detection and quantification, respectively. For GPE optimisation experiments, method A1 was used unless specified otherwise.    For the Orbitrap Eclipse the E1 method (30 MS2 windows of 20 Th each) and E2 method (60 MS2 windows of 10 Th each) were developed for the Eclipse Tribrid from recommended DIA methods on Xcalibur. These were used alongside method E3 (an in-house HeLa-optimised method, featuring 45 variable-width MS2 windows).  The timsTOF Pro MS was operated in diaPASEF mode through Compass Hystar 5.1, and three methods were set up directly via  the instrument software (timsTOF control 2.0.18.0) . Firstly, method T1 was a narrow polygon-based thin-PASEF method (Ryo et al., 2024) centred around the +2 precursor density region, first implemented based on an original 30-minute neat plasma injection which covered the 380-980 m/z and 0.6-1.1 1/K0 regions. Method T1 was created using the Bruker Compass HyStar window editor. Method T2 was an optimised py-diAID window method (Skowronek et al., 2022) for plasma, also developed on a 30-minute neat plasma injection as per method T1. Lastly, method T3 was based on an in-house optimised method of two windows in each diaPASEF scan across 16 × 25 m/z precursor isolation windows (32 windows) defined from m/z 400 to 1,200, with 1 Da overlap, and CID collision energy ramped stepwise from 20 eV at 0.8 V·s/cm2 to 59 eV at 1.3 V·s/cm2."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Library-free data searches were performed using Spectronaut v19.0 (Biognosys) (Bruderer et al., 2015) or DIA-NN v1.9 (Demichev et al., 2020), with the following configurations: Spectronaut v19.0 searches used Direct DIA™, the protein false discovery rate (FDR) was set to 1%, referencing the UniProt-reviewed human FASTA file (July 2022, 20,663 protein genes), which included Biognosys iRT peptides and E. coli β-galactosidase. These searches were conducted in alignment with the experimental design: for benchmarking, contamination (%PRP) was specified as a “condition” in Spectronaut, and searches were separated by method (MS, gradient, and DIA scheme)."],"omics_type":["Proteomics"],"labhead":["Laura Dagley"],"instrument_platform":[""],"labhead_affiliation":["Lab Head: WEHI"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["jack.edw02@gmail.com"],"publication":["41987532 Edwards J, Multari DH, Dite T, Binos S, Shugg C, Webb AI, Dagley LF, Emery-Corbin SJ. Plasma Proteomics Across Three Generations of Mass Spectrometry Instruments: Lessons for Biofluid Method Optimisation. Proteomics. 2026:e70127 10.1002/pmic.70127"],"submitter_affiliation":["WEHI, CSL Seqirus"],"submitter_country":["Australia"],"pubmed_abstract":["In biomarker discovery phases clinical proteomics provides large-scale identification and quantification of proteins in donor samples. For these studies plasma is the most frequently used biofluid, as it reflects both physiological and pathological states of the circulating proteome. However, the vast dynamic range of proteins in plasma remains a significant challenge, where low-abundance biomarkers are suppressed by high-abundance proteins, despite substantial technological improvements. Often the focus of improving outcomes in plasma proteomic workflows are within the biofluid's sample preparation, although adjusting MS methods dramatically improves detection and sampling of lower abundance proteins. Herein we have benchmarked various liquid chromatography (LC) and data-independent acquisition (DIA) methods across three generations of mass spectrometry instruments: timsTOF Pro (2017), Orbitrap Eclipse (2020), and Orbitrap Astral (2023). This study explored 27 combinations of LC-MS methods across 200 hours of instrument acquisition time, encompassing varying LC and MS settings. While each instrument generation significantly improved performance, each instrument also revealed a unique and different tuneable range to improve performance in plasma samples, highlighting the benefit of investing in plasma-specific method development for any mass spectrometer. We also evaluated the detection and quantification capabilities of each instrument via a unique approach of mixing paired platelet poor plasma (PPP) and platelet rich plasma (PRP), introducing linear contamination markers for quantitative assessment. This approach tested each instrument's sensitivity to detect low-abundance peptides and evaluated their quantitative accuracy. Lastly, we performed testing of the Orbitrap Astral's parallel ion processing capabilities with the aim of improving low-abundance protein identifications using gas-phase enrichment (GPE). More specifically, we show that optimisation of MS2 AGC targets and injection time enhanced GPE of low-abundance peptides, improving detection in plasma samples."],"pubmed_title":["Plasma Proteomics Across Three Generations of Mass Spectrometry Instruments: Lessons for Biofluid Method Optimisation."],"pubmed_authors":["Edwards Jack J, Multari Dylan H DH, Dite Toby T, Binos Steve S, Shugg Clare C, Webb Andrew I AI, Dagley Laura F LF, Emery-Corbin Samantha J SJ"],"additional_accession":[]},"is_claimable":false,"name":"Plasma Proteomics Benchmarking and Optimisation/ Plasma proteomics across three generations of mass spectrometry instruments: lessons for optimising biomarker discovery","description":"In biomarker discovery phases clinical proteomics provides large-scale identification and quantification of proteins in donor samples. For these studies plasma is the most frequently used biofluid, as it reflects both physiological and pathological states of the circulating proteome. However, the vast dynamic range of proteins in plasma remains a significant challenge, where low-abundance biomarkers are suppressed by high-abundance proteins, despite substantial technological improvements. Often the focus of improving outcomes in plasma proteomic workflows are within the biofluid’s sample preparation, although adjusting MS methods dramatically improves detection and sampling of lower abundance proteins. Herein we have benchmarked various liquid chromatography (LC) and data-independent acquisition (DIA) methods across three generations of mass spectrometry instruments: timsTOF Pro (2017), Orbitrap Eclipse (2020), and Orbitrap Astral (2023). This study explored 27 methods across 200 hours of instrument acquisition time, encompassing varying LC, MS, and database searching workflows. While each instrument generation significantly improved performance, each instrument also revealed a unique and different tuneable range to improve performance in plasma samples, highlighting the benefit of investing in plasma-specific method development for any mass spectrometer. We also evaluated the detection and quantification capabilities of each instrument via a unique approach of mixing paired Platelet Poor Plasma (PPP) and Platelet Rich Plasma (PRP), introducing linear contamination markers for quantitative assessment. This approach tested each instrument's sensitivity to detect low-abundance peptides and evaluated their quantitative accuracy. Lastly, we performed testing of the Orbitrap Astral’s parallel ion processing capabilities with the aim of improving low-abundance protein identifications using gas-phase enrichment (GPE). More specifically, we show that optimisation of MS2 AGC targets and injection time enhanced GPE of low-abundance peptides, improving detection in plasma samples.","dates":{"publication":"2026-04-21","submission":"2025-10-02"},"accession":"PXD069060","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:247480","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:1599","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:294671","NEWT:376619","NEWT:1748418","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:4615","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:2086595","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:381198","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:3357","NEWT:7719","NEWT:29073","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:2020713","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:2502409","NEWT:212790","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:370038","NEWT:498211","NEWT:345076","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:200795","NEWT:342808","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:329854","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:2649329","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:3715","NEWT:2065263","NEWT:199225","NEWT:177437","NEWT:717966","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:10886","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:1955249","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:2714896","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:1608994","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:1122981","NEWT:2853422","NEWT:1122984","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:2836","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:119562","NEWT:1883446","NEWT:31345","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:1922344","NEWT:108458","NEWT:5936","NEWT:85692","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:279010","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:415978","NEWT:235455","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:9054","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:717989","NEWT:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166314","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:1871049","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:548","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:2126348","NEWT:5180","NEWT:256737","NEWT:299467","NEWT:9541","NEWT:51350","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:542","NEWT:2903","NEWT:185579","NEWT:872227","NEWT:13076","NEWT:2587410","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:2126337","NEWT:550","NEWT:253237","NEWT:10804","NEWT:33941","NEWT:554","NEWT:451516","NEWT:552","N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