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Østergaard"],"technology_type":["Mass Spectrometry","Bottom-up proteomics","Data-independent acquisition"],"disease":["Disease Free"],"software":["Not available"],"submitter_keywords":["Enrichment strategies","Data independent acquisition","Plasma proteomics","Depletion strategies","Extracellular vesicles","Workflow assessment","Mass spectrometry","Astral"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070324"],"tissue":["Blood Plasma","Blood Serum"],"sample_protocol":["Samples were collected from anonymous adult healthy blood donors in 4 mL K2-EDTA tubes and cent. 6 min, 2000g for platelet-rich plasma (PRP) or 3000g for platelet-poor plasma (PPP). Serum (SER) were collected in 4 mL dry tubes, left to coagulate for 30 min and cent. 6 min, 2000g. All samples were cent. within 2 hours post collection, aliquoted and frozen at -80 °C until analysis. Neat plasma were denatured, reduced and alkylated in sample buffer (4% SDS, 100 mM TrisHCl pH 8.0 with 5 mM TCEP and 10 mM CAA; 1% SDS final concentration) for 15 min at 37 °C. The samples were then diluted 250X with PBS. Top14 protein depletion were performed by mixing 5 uL sample with 200 uL Depletion Resin (High-Select™ Top14 Abundant Protein Depletion Resin, Cat# A36372, Rockford, IL) in 96-well filter plates (Millipore, Cat# MSHVN45) and incubation 10 min, RT with frequent mixing. The samples were then cent. 2 min, 800g, and 30 uL sample was transferred to a new 96-well plate with 90 uL sample buffer for reduction and alkylation.  In the acid precipitation workflow (PerCA), 50 uL sample was mixed with 450 uL Milli-Q and 25 uL 70% Perchloric Acid (PerCA; final conc. 3.5%) before incubation at -20 °C, 15 min. After cent. 3,200g, 60 min, 4 °C, 250 uL supernatant was mixed with 40 uL 1% TFA and loaded on a uSPE HLB plate (Waters, Cat# 186001828BA) following the manufacturer’s instructions. Proteins were eluted with 90% ACN, 0.1% TFA and speedvac’ed to dryness. The dried pellets were resuspended in 35 uL 50 mM ammonium bicarbonate (ABC), 5 mM TCEP, 10 mM CAA before digestion with trypsin and eLysC.  In the workflow for acid precipitation with neutralization using NaOH (PerCAN), 10 uL sample was diluted with 40 uL Milli-Q water in a 96-well plate before addition of 50 uL 1.0 M PerCA and incubation at 4 °C, 60 min. After cent. 60 min, 4,000g, 4 °C, 48 uL supernatant was transferred to a new plate and mixed with 16 uL 1.4 M NaOH. Subsequently, reduction and alkylation were performed by addition of a tetra-ethyl ammonium bicarbonate (TEAB) based buffer (60 mM) supplemented with 5 mM TCEP, 10 mM CAA and incubated at 95 °C, 10 min before cooling and addition of trypsin and eLysC.  For the SAX bead enrichment (SAX) workflow, 20 uL or 40 uL sample was diluted 1:2 with binding buffer (100 mM Bis-Tris Propane, pH 6.3, 150 mM NaCl) in a 96-well plate. Then 100 ug (5 uL) SAX beads (ReSyn Bioscience, South Africa) in binding buffer were added before incubating 60 min on a thermoshaker, 600 rpm, RT. The supernatant was removed using a magnetic rack and the beads were washed 3X with 50 mM Bis-Tris Propane, pH 6.5, 150 mM NaCl. The beads were then resuspended in 50 uL sample buffer and incubated for 15 min, 37 °C to complete reduction and alkylation. For the enrichment of extracellular vesicles (EVs) by ultracentrifugation (EV20k), 500 uL sample was transferred to 1.7 mL tubes and mixed with 500 uL PBS. Tubes were cent. 3000g, 2.5 min to remove remaining platelet or coagulates and the supernatant was transferred to a new tube. The samples were then cent. 20,000g, 30 min to pellet EVs followed by discarding the supernatant except for 20 uL above the pellet. After addition of 980 uL PBS, the cent. was repeated leaving again 20 uL supernatant with the EV20k pellet. The pellets were then incubated with sample buffer for 15 min, 37 °C to complete reduction and alkylation. With exception of the PerCA and PerCAN samples, the samples subject to the neat, enrichment or depletion workflows were digested using our protein aggregation capture protocol (Batth et al., 2019), desalted and loaded on EvoTips (EvoTips, Evosep Biosciences, Denmark) using an OT2 Opentron robot. For the automated workflow, 5 uL sample was diluted to approx. 0.5 ug/uL, transferred to a sample plate together with 100 ng Hydroxyl-beads (ReSyn Biosciences) and placed on the OT2 robot. The Opentron was set to load approximately 500 ng peptide per EvoTip. For the SAX samples, 10 uL sample (including 20 ng SAX beads) were used without Hydroxyl-Beads. The PerCA and PerCAN samples were digested in 50 mM ABC or in 60 mM TEAB buffer and manually loaded onto EvoTips. Peptides were eluted from EvoTips using an Evosep One LC system and separated using an 8 cm column (EV1109, Evosep) connected to a steel emitter (EV1086, Evosep) and heated to 40 °C over an 11 min or 21 min gradient. The eluted peptides were electrosprayed into an Orbitrap Astral mass spectrometer using 1800 V spray voltage, funnel radio frequency level 40, and a heated capillary temperature at 275 °C in positive mode. Full scan precursor spectra (380–980 Da) were recorded in profile mode at 240k resolution, an AGC target of 500%, and a max injection time (IT) of 3 ms. Fragment spectra were acquired in the m/z range 380-980 Da with 2 Th isolation windows without overlap. Isolated precursors were fragmented in the HCD cell using 25% normalized collision energy, a normalized AGC target of 500%, and a max IT of 2.5 ms."],"repository":["pride"],"quantification_method":[""],"modification":[""],"data_protocol":["The mass spectrometry generated RAW-files were analyzed using DIANN v2.2.0 (academia) searching against a FASTA file containing the human proteome (SwissProt, 20,421 sequences, downloaded on May 6th, 2025) plus two amino acid sequences from the applied proteolytic enzymes (trypsin and lysylendopeptidase C) in a two step process. First, DIANN was used to generate an in silico spectral library from the applied FASTA files. Secondly, DIANN was applied for searching the generated raw-files against the spectral library generated. Carbamidomethyl, N-terminal acetylation and oxidation of methionine were allowed as potential modifications. A maximum of one variable modification was allowed. Trypsin was specified as the proteolytic enzyme with a maximum of one missed cleavage allowed. The peptide range was set to 7-30 amino acids, the precursor charge to 2-5, the precursor m/z range to 380-980 m/z and the fragment ion m/z range to 150-2000 Da. The peptideThe mass tolerance was set to automatic inference at both MS1 and MS2 levels with a precursor FDR level at 1%. Quantification was performed using the Quant UMS (high precision) setting . Intensity-Based Absolute Quantification (IBAQ) was calculated after the DIANN search by dividing the label-free quantification by the number of theoretical peptides for each protein group."],"omics_type":["Proteomics"],"labhead":["Jesper Velgaard Olsen"],"instrument_platform":[""],"labhead_affiliation":["Novo Nordisk Foundation, Center for Protein Research Faculty of Health and Medical Sciences University of Copenhagen Blegdamsvej 3B,  DK-2200 Copenhagen N Denmark"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["ole.ostergaard@cpr.ku.dk"],"publication":["42068309 Kverneland AH,Østergaard O,Schmidt L,Østergaard Johansen M,Ullitz Thorsen S,Frikke Schmidt R,Christoffersen C,Olsen JV Benchmarking Plasma Proteomics Workflows and Their Correlation to Clinical Routine Protein Assays. J Proteome Res. 2026 May 2 10.1021/acs.jproteome.6c00078"],"submitter_affiliation":["Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences\nUniversity of Copenhagen, Blegdamsvej 3B,  DK-2200 Copenhagen N, Denmark"],"submitter_country":["Denmark"],"additional_accession":[]},"is_claimable":false,"name":"Benchmarking workflows for plasma proteomics","description":"In this project we asses 5 different sample processing workflows for mass spectrometry based plasma proteomics and compare the results with a neat plasma workflow. The workflows evaluated includes protocols for abundant protein depletion (Top14 most abundant protein depletion and protein precipitation by perchloric acid) and enrichment for low abundant proteins (SAX based enrichment of low abundant proteins and ultracentrifugation based enrichment for extracellular vesicles). The assessment comprises two steps: In the first step, each workflow is repeated 8X on the same input material from one donor and focuses on proteomic depth and precision of protein quantifications. In addition, the effect of three different input materials in the form of platelet poor plasma (PPP), platelet rich plasma (PRP) and serum (SER) is evaluated. In the second step, samples from 72 healthy donors is evaluated 1X in SER and in PPP or PRP, and in addition, levels of 10 proteins--commonly measured in clinical practise and spanning 5 orders of magnitude in abundance--is quantified by a clinical rutine measurement performed at a Cobas system. Focus is again proteomic depth obtained by the evaluated methods, and in addition focus is on how well the estimates by the clinical rutine measurements in SER correlate with the mass spectrometry based estimates after sample processing by the 6 assessed workflows in all three input types (PPP. PRP, SER).","dates":{"publication":"2026-05-04","submission":"2025-11-05"},"accession":"PXD070324","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","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:376619","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: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:7719","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","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:2579791","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","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:270643","NEWT:3715","NEWT:2065263","NEWT:177437","NEWT:717966","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","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:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:2853422","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: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:108458","NEWT:5936","NEWT:85692","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:415978","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","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:9541","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:10804","NEWT:33941","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:575412","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT: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