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Wallner"],"technology_type":["Mass Spectrometry","Bottom-up proteomics","Data-independent acquisition"],"software":[""],"submitter_keywords":["Automation","Sample preparation","Proteomics","Nlc-ms/ms","Centrifugal microfluidics","Personalized medicine"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD072920"],"tissue":["Cell Culture"],"sample_protocol":["Carboxylated-modified SpeedBeads (Cytiva, GE65152105050250, GE45152105050250) at a protein:bead ratio of 1:10 w/w were used in the manual and KingFisher workflow. Beads were pre-washed three times with ddH2O and resuspended in with their working volume prior use. Proteins were precipitated by addition of ethanol to a final concentration of 70 % ethanol (v/v) and incubation for binding (10 min at 1000 rpm, room temperature, in the manual workflow; 30 minutes on the KingFisher workflow). Beads were then captured magnetically (rack for manual; instrument magnets for KingFisher), and the supernatant was removed and discarded. In the manual protocol, beads were washed three times with 200 µL of 80 % ethanol (Roth, 5054.3), followed by brief air-drying step (5 minutes, open tube) to remove residual ethanol. In the KingFisher workflow beads were washed three times with 250 µL of 80 % ethanol (Roth, 9065.2). For on-bead digestion, beads were resuspended in ammonium biocarbonate buffer (manual: 100 mM ABC (Sigma-Aldrich, 09830-500G), pH 8.0; KingFisher: 50 mM ABC (Roth, T817)), and sequencing-grade trypsin (Promega, V5111) was added at a protein:enzyme ratio of 1:25 (w/w). Digestion proceeded at 37 °C (manual: 4 hours at 1000 rpm on a thermoshaker; KingFisher: overnight at 650 rpm on a thermoshaker). For the manual workflow, the reaction was stopped by acidification to a final concentration of 1 % TFA (Merck, 1082180050) and the acidified digest supernatant was transferred to a new tube, centrifuged at full speed for 10 min, and the clarified supernatant was transferred again to a fresh tube to avoid bead carry-over before drying in a vacuum concentrator at 45 °C and storage at -80 °C. In the KingFisher workflow, beads were additionally washed with 2 % TFA (Th. Geyer, 044630.AP) to recover residual peptides, and both eluates were combined with a final concentration of 1 % TFA. For peptide quantification in the manual workflow, dried peptides were resuspended in 60 µL 0.1 % formic acid (FA) and analyzed using a fluorescence-based peptide assay (Thermo Fisher Scientific, 23290). To avoid carry-over of beads on the UHPLC-system, KingFisher samples were cleaned up using the previously described stage-tip protocol29. As an initial step for preparing the AutoPAC-Disk, 20 µL of the 25 % Pure Cube (Cube Biotech, 50201) beads suspension were washed twice with 1 mL of PBS (Gibco, 20012-019) and once with 1 mL ddH2O. After washing, the beads were resuspended in 80 µL ddH2O for loading into the bead inlet. Subsequently, 50 µL of reduced and alkylated protein lysate was pipetted into the sample inlet, followed by digestion mix consisting of 10 µL 100 mM ammonium bicarbonate buffer (pH 8) (Sigma-Aldrich, 09830-500G) and 4 µL sequencing grade modified trypsin with a 1:25 (protein:enzyme) w/w ratio (Promega, V5111) into the respective inlet. The AutoPAC-Disk was processed on the Rhonda player developed by Hahn Schickard, Dialunox and Spindiag. All experiments were performed on a test rig equipped with a stroboscopic set-up (Hamilton, Germany) to monitor liquid movement in real time. Once the disk was inserted into the Rhonda player a pre-defined protocol that controls rotational frequency as well as temperature of the ten different heating zones of the player was executed to perform the automated workflow. DIA raw files were converted to .mzML using MSConvertGui (peak Picking vendor msLevel =1-, zeroSamples removeExtra 1-) (ProteoWizard30). mzML files were searched using FragPipe v23.131. Only replicates were searched together. Decoys and contaminants were added to a human FASTA, based on the swissprot entries from January 2024, containing protein isoforms. MSFragger (version 4.331) was used for identification (protein digestion: stricttrypsin; variable modification: oxidation on methionine and protein nN-terminal acetylation; fixed modification: carbamidomethylation on cysteines). Quantification was performed using DIA-NN v1.8.132 without normalization (--no-norm)."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["DIA raw files were converted to .mzML using MSConvertGui (peak Picking vendor msLevel =1-, zeroSamples removeExtra 1-) (ProteoWizard30). mzML files were searched using FragPipe v23.131. Only replicates were searched together. Decoys and contaminants were added to a human FASTA, based on the swissprot entries from January 2024, containing protein isoforms. MSFragger (version 4.331) was used for identification (protein digestion: stricttrypsin; variable modification: oxidation on methionine and protein nN-terminal acetylation; fixed modification: carbamidomethylation on cysteines). Quantification was performed using DIA-NN v1.8.132 without normalization (--no-norm).  The report.tsv, report.pr_matrix.tsv and report.pg_matrix.tsv MSFragger output files were used. All files were processed in R33 and RStudio34. Data was visualized using ggplot235. Physicochemical properties of peptides and protein groups were analyzed using Peptides36. All analyses were restricted to peptides and protein groups that were identified and quantified. Coefficients of variations (CVs) were calculated on protein group level including all identified and quantified protein groups. Beforehand, LFQ intensities were normalized on the overall median."],"omics_type":["Proteomics"],"labhead":["Hannes Hahne"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["OmicScouts, a Momentum Biotechnologies Company"],"species":["Homo Sapiens (human)"],"publication":["10.1039/D6LC00211K"],"submitter_mail":["johanna.wallner@tum.de"],"submitter_affiliation":["Technical University of Munich"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"Centrifugal microfluidic automation of the protein aggregation capture workflow for robust mass spectrometry-based proteomics","description":"Proteomic sample preparation for liquid chromatography-tandem mass spectrometry (LC-MS/MS) is increasingly addressed by automated approaches. However, in clinical settings, where only a limited amount of samples has to be processed in a standardized and reproducible manner, no fully automized workflow was provided yet. remains a major bottleneck for the broader adoption of clinical and translational proteomics due to its labor-intensive and error-prone nature. Here, we present the AutoPAC-Disk, a centrifugal microfluidic implementation of a protein aggregation capture (PAC) sample preparation workflow for bottom-up proteomics. The AutoPAC-Disk features a bead-packed column with a miniaturized digestion volume of 14 µL and pre-stored organic solvents. A comparative evaluation using HEK293 cell lysates revealed higher identification rates than both a manual commonly used reference workflow and a its semi-automated robotic system implementation (KingFisher), yielding 50 % and 37 % more peptide identifications and 23 % and 10 % more protein identifications, respectively. These gains in peptide identifications translated into increased sequence coverage of the identified proteins. Quantitative reproducibility was high for all approaches, with medianOur AutoPAC-Disk resulted in a similar exhibits high quantitative reproducibility with protein group intensity coefficients of variation below 10 %, similar to the other well -established workflows. Further analysis revealed that the AutoPAC-Disk predominantly enabled additional protein identifications in the low-abundance range. Together, these results provide a proof of concept that microfluidic automation, including the successful on-disk pre-storage of reagents and buffers, can substantially simplify proteomic sample preparation by enabling a high degree of automation and minimal user interaction. This approach lowers the operational barrier for personnel with limited experience in proteomic sample preparation and represents a promising strategy for future applications in clinical and translational proteomics within the field of precision medicine.","dates":{"publication":"2026-06-29","submission":"2026-01-12"},"accession":"PXD072920","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:111205","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","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:2492962","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:3357","NEWT:111225","NEWT:7719","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:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:2502409","NEWT:212790","NEWT:110368","NEWT:55350","NEWT:1916073","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:1912919","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:156587","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:270643","NEWT:3715","NEWT:1538","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:2714896","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:1608994","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2709072","NEWT:2499525","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:294607","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: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: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:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166314","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","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: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:132529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