{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070862/ALDH1A3_ARS_1620_psm.tsv"],"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070862/ARS_1620_SPROX.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070862/ARS_1620_high_1.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070862/ARS_1620_TPP.msf"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070862/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070862/ARS_1620_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070862/ARS_1620_high_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070862/ARS_1620_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070862/ARS_1620_high_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070862/ARS_1620_high_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070862/ARS_1620_Enrich1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070862/ARS_1620_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070862/ARS_1620_Enrich4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070862/ARS_1620_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070862/ARS_1620_high_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070862/ARS_1620_Enrich2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070862/ARS_1620_Enrich3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070862/ALDH1A3_ARS1620.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070862/ALDH1A3.fasta"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070862/ARS_1620_high_1.pdResult","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070862/ARS_1620_SPROX.pdStudy","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070862/ARS_1620_TPP.pdStudy","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070862/ARS_1620_SPROX_Met_Enrich.pdResult","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070862/ARS_1620_TPP.pdResult","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070862/ARS1620_2026_04_26.pdStudy"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["michael.c.fitzgerald@duke.edu"],"submitter":["You Zou"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"disease":["Non-small Cell Lung Carcinoma"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070862"],"tissue":["Epithelial Cell","Cell Culture"],"sample_protocol":["One-pot SPROX Analysis H358 cell lysates were incubated with either DMSO (vehicle), 10 μM ARS-1620, or 100 uM ARS-1620 for 4 hours at room temperature. The resulting lysates were analyzed using a one-pot SPROX workflow as previously described.1 Briefly, each lysate was divided into aliquots and further distributed into 12 phosphate-buffered saline (PBS, pH 7.4) solutions containing increasing urea concentrations (0.5 - 6.0 M, in 0.5 M increments). The samples were equilibrated for 2 h at room temperature. Subsequently, 3 μL of 30% (w/w) hydrogen peroxide was added to 30 μL of each equilibrated  sample to initiate methionine oxidation. After 3 min, the reactions were quenched with 150 μL of 1.0 M TCEP (pH 7.0). All urea-denatured samples corresponding to each treatment replicates were polled to generate a single “one pot” sample. The resulting protein mixtures were processed using the iFASP protocol (ref) and labelled with isobaric TMT 10-plex reagents. Methionine-containing peptides were enriched using the Pi3 methionine reagent kit according to the manufacturer’s instructions, desalted on C18 Macrospin column, and analyzed in quadruplicates by LC-MS/MS.  One-pot TPP Analysis The same lysate samples described in one-pot SPROX protocol were subjected to a one-pot TPP analysis as previously described.1 Aliquots containing 10 μg of proteins were distributed into 10 tubes and heated for 3 min at one of 10 temperatures (low temperature: 37 - 64 °C, in 3 °C increments; high temperature: 46 - 73 °C, in 3 °C increments). Samples were then equilibrated at room temperature for 3 min prior to placed on ice. All temperature-treated aliquots for each condition were combined to yield a single  “one-pot” sample,  which was centrifuged at 48 000 rpm for 20 min at 4 °C. The supernatants were transferred into a 10 kDa MWCO centrifugal filter and processed following the iFASP protocol, as described for the SPROX analysis. Desalted peptides were analyzed in quadruplicate by LC-MS/MS.  Bottom-up Analysis of ALDH1A3-ARS1620 Covalent Adducts Recombinant His-tagged human ALDH1A3 protein (10 µM) was incubated with 100 µM ARS-1620 overnight at room temperature. The reaction mixture was subsequently digested with pepsin (enzyme-to-protein ratio 1:1; Sigma-Aldrich) at 37 °C and pH 2 for 1 hour. Resulting peptides were desalted using C18 ZipTips following the manufacturer’s instructions and dried to completeness using a SpeedVac. The dried peptides were stored at -80 °C until LC-MS/MS analysis.  Quantitative LC–MS/MS Analysis of SPROX and TPP sample  LC–MS/MS experiments were performed on a Thermo Orbitrap Exploris 480 mass spectrometer system coupled to a Thermo Easy-nLC 1200 system. Peptides were reconstituted in 2% acetonitrile and 1% trifluoroacetic acid (TFA) to 1 μg/μL, and 1 μg was injected per run. Peptides were trapped on a Thermo Acclaim PepMap 100 (75 μm × 2 cm) column and separated on a nanoViper 2Pk C18 (3 μm, 100 Å, 75 μm × 25 cm) analytical column using a 110 min linear gradient of 3–30% ACN at a flow rate of 400 nL/min and a column temperature of 45 °C. Data was acquired in data-dependent acquisition (DDA) mode with a top-20 method and 2.5 s cycle time. MS1 and MS2 scans were acquired at resolutions of 120k and 50k, respectively. The MS1 AGC target was 4.0 × 105 ions with a max injection time of 105 ms. HCD collision energy was set to 38%, with a scan range of 375–1500 m/z, an isolation window was 0.7 Da, and a dynamic exclusion duration of 60 s.  LC–MS/MS Analysis of ALDH1A3-ARS1620 adduct peptides LC–MS/MS analysis of ALDH1A3-ARS1620 adduct peptides was performed under conditions similar to those described for SPROX and TPP samples, except that a 40-minute linear acetonitrile gradient was used. The MS1 scan range was set to 250–1500 m/z, and the MS2 scan range was set to 105–1500 m/z."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["proteomics data analysis of SPROX and TPP sample Raw LC-MS/MS data were searched against mammalian protein databases (UniProt Knowledgebase 2017-10-25 release) using Proteome Discoverer 2.3 (Thermo) with the SEQUEST HT search engine. Search parameters included  fixed MMTS modification of cysteine, TMT 10-plex labeling of lysine side chains and peptide N-termini, and variable modification for methionine oxidation, and acetylation, Met-loss and Met-loss + cetylation of the protein N-terminus. Trypsin was specified as the protease with up to two missed cleavages allowed. Protein and peptide with an FDR confidence of “high” and “medium” (i.e., FDR < 1%) and without a single quantification channel of 0 were used for further processing.   The searched data was processed using a previously described procedure. For SPROX, the quantified TMT intensities were normalized by the average intensities of all methionine containing peptides for each channel to correct for labeling or sample-handling variability). Welch’s t-test was applied to the normalized data, and hits were defined as those with p-value <0.05 and log2(fold change) > 0.3 or < -0.3.  Proteomics data analysis of ALDH1A3-ARS1620 adduct peptides Raw LC–MS/MS data from ALDH1A3–ARS1620 adduct peptide samples were analyzed against the ALDH1A3 FASTA database using FragPipe v23.0, incorporating MSFragger 4.3, IonQuant 1.11.11, and Philosopher 4.8.1 search engines.2 The integrated FragPipe contaminant database was included to exclude potential contaminants. Precursor and fragment mass tolerances were both set to 20 ppm. Enzyme specificity was set to nonspecific cleavage, and peptide lengths between 3 and 30 amino acids were permitted. Variable modifications included oxidation of methionine and ARS-1620 adduction (+430.1008 Da) on cysteine residues. The false discovery rate (FDR) for peptide-spectrum matches (PSMs) and proteins was controlled at 1% using a target-decoy strategy. All other parameters were maintained at default settings. Search results were visualized using the integrated FragPipe peptide data viewer (FP-PDV).3"],"omics_type":["Proteomics"],"labhead":["Michael C."],"instrument_platform":[""],"labhead_affiliation":["Professor & Chair Chemistry Department  Duke University"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["yz785@duke.edu"],"publication":["Not available"],"submitter_affiliation":["Duke University"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Application of folding stability-based proteomics to profile cancer drug","description":"Covalent inhibitors offer powerful therapeutic advantages but require comprehensive profiling to define their on- and off-target activities. Here, we apply two stability-based proteomic methods, SPROX and TPP, to characterize protein targets of the KRASG12C inhibitor ARS-1620 in H358 cell lysate. Both methods identified ligand-induced protein stability shifts, collectively recovering the known on-target KRAS as well as multiple off-targets. Comparative analyses with ABPP and pull-down datasets highlighted ALDH1A3 as a reproducible off-target. Bottom-up proteomics mapped Cys314 as the major ARS-1620 modification site on ALDH1A3, and enzymatic assays confirmed dose-dependent inhibition. Covalent docking supported a favorable binding pose within the retinal-binding pocket. Together, these findings demonstrate that stability-based proteomics provides an effective, derivatization-free strategy for covalent drug target identification.","dates":{"publication":"2026-05-08","submission":"2025-11-18"},"accession":"PXD070862","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:1073882","NEWT:475174","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:383379","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:7719","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:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:2065263","NEWT:177437","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:244366","NEWT:1246791","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2853422","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:460523","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:108458","NEWT:5936","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:1255228","NEWT:410289","NEWT:373153","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:470","NEWT:5911","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:906914","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:6493","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:8655","NEWT:5147","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:40674","NEWT:1194669","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:80863","NEWT:90675","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:1123869","NEWT:9544","NEWT:9545","NEWT:979","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:305959","NEWT:13489","NEWT:29829","NEWT:92867","NEWT:92866","NCBITaxon:3055","NEWT:51750","NEWT:202950","NEWT:295027","NCBITaxon:11320","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:90690","NEWT:1436183","NEWT:300273","NEWT:4232","NEWT:416348","NEWT:11298","NEWT:4236","NEWT:7742","NEWT:196627","NEWT:200308","NEWT:200302","NEWT:870435","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:2666255","NEWT:999810","NCBITaxon:5693","NEWT:28995","NEWT:1392998","NEWT:380394","NEWT:226900","NEWT:1266738","NEWT:231490","NEWT:244704","NEWT:7725","NEWT:9909","NEWT:9902","NEWT:430615","NEWT:72664","NEWT:563041","NEWT:36599","NEWT:41949","NEWT:326423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