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Vignane"],"technology_type":["Mass Spectrometry","Shotgun proteomics"],"software":["Not available"],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD045806"],"tissue":["Brain","Frontal Lobe"],"sample_protocol":["Persulfidation enrichment for proteomic analysis The brain frontal cortexes were lysed in cold HEN Buffer (50 mM HEPES, 1 mM EDTA, 0.1 mM Neocuproine, 1 % IGEPAL, 2 % SDS, pH 7.4) supplemented with 5 mM 4-Chloro-7-nitrobenzofurazan (NBF-Cl, Sigma, #163260). Frozen tissue was disrupted in lysis buffer using the TissueLyser II and 5 mm stainless steel beads. Lysates were incubated for 2 h at 37°C. Proteins were precipitated twice using methanol/chloroform precipitation, and pellets were washed twice with cold methanol. To circumvent unspecific enrichment, samples were cleaned from endogenously biotinylated proteins. Shortly, pellets were resuspended in PBS + 0.2 % SDS and an equal amount of protein was incubated with Pierce™ NeutrAvidin™ Agarose beads (Thermofisher, #29200). After 2 h of mixing at room temperature (RT), supernatants were collected and precipitated once using methanol/chloroform precipitation. Pellets were resuspended in PBS + 2% SDS and proteins were incubated for 1.5 h at 37°C with 250 µM DCP-Bio1 (MERK, #NS1226). To remove the DCP-Bio1 excess, proteins were precipitated twice and washed using the previously described method. After precipitation, pellets were resuspended in PBS + 0.1 % SDS for protein estimation. Equal amountsof protein were incubated with Pierce™ High Capacity Streptavidin Agarose beads (Thermofisher, #20357) and mixed at RT for 4 h. Beads were then collected and transferred into 2 mL Pierce™ Disposable Columns  (Thermofisher, #29920) and washed with 28 ml of PBS and 8 ml of water to remove unspecific bindings and detergent. After washing, enriched proteins were eluted by incubating beads overnight with 2.25 M of Ammonia solution (Sigma, #5.33003) and collected the following morning for lyophilization. Lyophilized samples were dissolved in digestion buffer (50 mM Ammonium Bicarbonate, 1 mM Calcium chloride) anddigested overnight using Trypsin (Promega, #V5117) at a Trypsin: protein ratio 1:20. The desalting step was performed following the manufacturer protocol using Supel™-Select HLB SPE Tube (Sigma, #54181-U). Shortly, Columns were conditioned with the elution solution (60% acetonitrile [ACN], 0.1 % Trifluoroacetic acid [TFA]) and washed twice with washing buffer (0.1 % TFA). Each sample was then loaded on the column using gravity flow. Cartridges were washed once with washing buffer by gravity flow followed by two-time gravity flow elution of the peptides using the elution buffer. Eluates were evaporated under vacuum to remove elution buffer until dryness. Peptides were dissolved in 0.1 % TFA, and digestion quality control was performed using an Ultimate 3000 Nano Ultra High-Pressure Chromatography (UPLC) system with a PepSwift Monolithic® Trap 200 µm * 5 mm (Thermo Fisher Scientific). Peptides were dissolved in 0.1 % TFA before being analyzed by high-resolution LC-MS/MS using an Ultimate 3000 Nano Ultra High-Pressure Chromatography (UPLC) system (Thermo Fisher Scientific) coupled with a Thermo LTQ Velos Mass Spectrometer via an EASY-spray (Thermo Fisher Scientific). Peptide separation was carried out with an Acclaim™ PepMap™ 100 C18 column (Thermo Fisher Scientific) using a 140 min non-linear gradient from 7 to 80 % B (0 min, 7 % B; 15 min 17 % B; 30 min, 30 % B; 120 min, 65 % B; 140 min 80 % B; B: 84 % Acetonitrile, 0.1 % Formic Acid) at a flow rate of 250 nL/min. The LTQ Velos was operated in a DDA mode, and MS1 survey scans were acquired from 300 to 2000 m/z at a resolution of 60 000 using the Orbitrap mode. The ten most intense peaks with a charge state ≥  2 were fragmented using Collision-induced dissociation (CID) at 35 %  and analyzed using Iontrap at a standard scan rate. The dynamic exclusion was set at 20 seconds.  Direct detection of Sufonylated peptides using LC/MS 50 µg of the NBF-labelled samples resuspended in PBS 2 % SDS (see section “PSSH enrichment for proteomic analysis”) were trypsinized over-night as described above. Samples were subjected to desalting and Pierce® Detergent Removal columns (ThermoFisher, # 87777). Peptides evaporated under vacuum until dryness as described above. Peptides were dissolved in 0.1 % TFA, and digestion quality was assessed as previously described. Peptides were analyzed by high-resolution LC-MS/MS using an Ultimate 3000 Nano Ultra High-Pressure Chromatography (UPLC) system (Thermo Fisher Scientific) coupled with an Orbitrap Eclipse™ Tribrid™ Mass Spectrometer via an EASY-spray (Thermo Fisher Scientific). Peptide separation was carried out with an Acclaim™ PepMap™ 100 C18 column (Thermo Fisher Scientific) using a 160 min linear gradient from 3 to 35 % of B (84 % Acetonitrile, 0.1 % Formic Acid) at a flow rate of 250 nL/min. The Orbitrap Eclipse™ was operated in a DDA mode, and MS1 survey scans were acquired from m/z 300 to 1,500 at a resolution of 120, 000 using the Orbitrap mode. MS2 scans were carried out for 3 seconds with high-energy collision-induced dissociation (HCD) at 32 % using the Normal speed IonTrap mode."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Persufidation data analysis Data were evaluated with PEAKS ONLINE software using 15 ppm for precursor mass tolerance, 0.5 Da for fragment mass tolerance, specific tryptic digest, and a maximum of 3 missed cleavages. NBF (+163.00961594 Da) on C, K, and R, and DCP (+168.0786442 Da) on C, N-term acetylation (+42.010565 Da), and methionine oxidation (+15.994915 Da) were added as variable modifications, peptide-spectrum match (PSM) and proteins were filtered at FDR 1 %. Samples were then normalized using the eigenMS script on R studio.   Direct detection of cysteine sulfonylation analysis Data were evaluated with PEAKS ONLINE software using 15 ppm for precursor mass tolerance, 0.5 Da for fragment mass tolerance, specific tryptic digest, and a maximum of 3 missed cleavages. NBF (+163.00961594 Da) on C, K, and R, Trioxidation (+47.984744 DA) on C, N-term acetylation (+42.010565 Da), and methionine oxidation (+15.994915 Da) were added as variable modifications, peptide-spectrum match (PSM) and proteins were filtered at FDR 1 %. Data sample were normalized to TIC."],"omics_type":["Proteomics"],"labhead":["Milos Filipovic"],"instrument_platform":[""],"labhead_affiliation":["SULFAGIN group, Leibniz-Institut für Analytische Wissenschaften, ISAS .eV, Germany"],"submission_type":["COMPLETE"],"species":["Mus Musculus (mouse)"],"publication":["Not available"],"submitter_mail":["thibaut.vignane@outlook.com"],"submitter_affiliation":["Leibniz-Institut für Analytische Wissenschaften - ISAS,e.V, Dortmund, Germany"],"submitter_country":["Germany"],"doi":["10.6019/PXD045806"],"additional_accession":[]},"is_claimable":false,"name":"Persulfidation and direct detection of sulfonylation in aging Brain of WT, CSE-/- and MPST-/- mice","description":"Cellular homeostasis relies on precise regulation through chemical processes, such as protein posttranslational modifications and physical processes, such as biomolecular condensation. Aging disrupts this balance, increasing susceptibility to diseases and death. However, the mechanisms behind age-related pathogenesis remain unclear. Using chemoproteomic methods to dissect different cysteine posttranslational modifications, we found that age-related changes in cysteine redox homeostasis impact proteins ability to form biomolecular condensates. Age-related increase in sulfenylation and sulfonylation promotes phase separation and through conformational change increases proteins propensity to aggregate. Causing condensates dissolution, protein persulfidation, a protective thiol modification, prevents this. Reduced persulfidation and increased sulfonylation in aging drive abnormal phase separation, leading to shorter life and spontaneous protein aggregation in CSE-/- mice.  In this study, we assessed the changes in protein persulfidation levels in brain aging. For this, we used the frontal cortex of 10 weeks, 10 months and 18 months-old WT mice . To unravel the protective role of H2S against ROS, we used the thiol-blocked samples from the persulfidation protocol to directly detect cysteine sulfonylation by mass spectrometry.","dates":{"publication":"2026-05-23","submission":"2023-09-29"},"accession":"PXD045806","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","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:270643","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: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