{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD032671/checksum.txt"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD032671/uniprot-sp_canonical_160322_PFAM_v03.12.15.fasta"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD032671/DKFZ-748_A_txt.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD032671/03_MaxQuant_1.6.1.0.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD032671/Vorinostat_B_txt.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD032671/DKFZ-748_B_raw.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD032671/Vorinostat_C_txt.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD032671/Vorinostat_C_raw.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD032671/CHDI00465983_B_raw.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD032671/File_description_PRIDE.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD032671/CHDI00465983_A_raw.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD032671/CHDI00465983_B_txt.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD032671/DKFZ-748_C_raw.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD032671/CHDI00465983_A_txt.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD032671/DKFZ-748_C_txt.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD032671/Vorinostat_B_raw.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD032671/Vorinostat_A_raw.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD032671/DKFZ-748_A_raw.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD032671/DKFZ-748_B_txt.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD032671/Vorinostat_A_txt.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["kuster@tum.de"],"submitter":["Severin Lechner"],"technology_type":["Affinity purification coupled with mass spectrometry proteomics","Mass Spectrometry","Shotgun proteomics"],"disease":["Brain Cancer"],"software":[""],"submitter_keywords":["Chemical biology","Histone deacetylase","Lc-ms/ms","Drug discovery","Polyamines","Chemical probes","Be(2)-c","Chemical proteomics"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD032671"],"sample_protocol":["Competition Pulldown assays. For the selectivity profiling of DKFZ-748, Vorinostat and CHDI00465983, lysate from BE(2)-C cells was used. Competition assays for DKFZ-748 and Vorinostat were performed in triplicates, and competition assays for CHDI00465983 in duplicates. 0.5 mL of the lysate (adjusted to 5 mg/mL protein concentration and 0.4% Igepal) was pre-incubated with 11 doses of inhibitor (DMSO vehicle, 3 nM, 10 nM, 30 nM, 100 nM, 300 nM, 1000 nM, 3000 nM, 10000 nM, 30000 nM, 100000 nM)  for 1 h at 30 °C in an end-over-end shaker, followed by incubation with 18 µL affinity matrix (1:1:1 mixture of iC, iQ and iA) ] for 30 min at 30 °C in an end-over-end shaker.  To assess the degree of protein depletion from lysates by the affinity matrix, a second pulldown (PDPD) with fresh beads was performed in six replicates, using the unbound protein fraction from the vehicle control flow through.  The beads were washed (1x 1 mL of lysis buffer without inhibitors and only 0.4% Igepal, 2x 2mL of lysis buffer without inhibitors and only 0.2% Igepal) and captured proteins were denatured with 8 M urea buffer, alkylated with 55 mM chloroacetamide and digested with Trypsin according to standard procedures. Resulting peptides were desalted on a C18 filter plate (Sep-Pak® tC18 µElution Plate, Waters), vacuum dried and stored at -20 °C until LC-MSMS measurement."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["LC-MSMS measurement of competition pulldown assays. Peptides were analyzed via LC-MS/MS on a Dionex Ultimate3000 nano HPLC coupled to an Orbitrap Fusion Lumos mass spectrometer (Thermo Fisher Scientific) mass spectrometer, run via the Thermo Scientific Xcalibur software. Peptides were loaded on a trap column (100 μm x 2 cm, packed in house with Reprosil-Gold C18 ODS-3 5 μm resin, Dr. Maisch, Ammerbuch) and washed with 5 μL/min solvent A (0.1 % formic acid in HPLC grade water) for 10 min. Peptides were then separated on an analytical column (75 μm x 40 cm, packed in house with Reprosil-Gold C18 3 μm resin, Dr. Maisch, Ammerbuch) using a 50 min gradient ranging from 4-32 % solvent B (0.1 % formic acid, 5 % DMSO in acetonitirile) in solvent A (0.1 % formic acid, 5 % DMSO in HPLC grade water) at a flow rate of 300 nL/min. The mass spectrometer was operated in data dependent mode, automatically switching between MS1 and MS2 spectra. MS1 spectra were acquired over a mass-to-charge (m/z) range of 360-1300 m/z at a resolution of 60,000 (at m/z 200) in the Orbitrap using a maximum injection time of 50 ms and an automatic gain control (AGC) target value of 4e5. Up to 12 peptide precursors were isolated (isolation width of 1.2 Th, maximum injection time of 75 ms, AGC value of 1e5), fragmented by HCD using 30 % normalized collision energy (NCE) and analyzed in the Orbitrap at a resolution of 30,000. The dynamic exclusion duration of fragmented precursor ions was set to 20 s. Competition Pulldown assay protein identification and quantification. Protein identification and quantification was performed using MaxQuant1 (v 1.6.1.0) by searching the LC-MS/MS data against all canonical protein sequences as annotated in the Swissprot reference database (v03.12.15, 20193 entries, downloaded 22.03.2016) using the embedded search engine Andromeda. Carbamidomethylated cysteine was set as fixed modification and oxidation of methionine and N-terminal protein acetylation as variable modifications. Trypsin/P was specified as the proteolytic enzyme and up to two missed cleavage sites were allowed. Precursor tolerance was set to 10 ppm and fragment ion tolerance to 20 ppm. The minimum length of amino acids was set to seven and all data were adjusted to 1% PSM and 1% protein FDR. Label-free quantification1 was performed with LFQ min. ratio count of 1 (unique and razor) and match between runs was enabled .  (Competition) Pulldown assay data analysis. For the competition assays, relative binding was calculated based on the protein intensity ratio relative to the DMSO control for every single inhibitor concentration.  EC50 values were derived from a four-parameter nonlinear regression with a fixed top plateau of 1 and variable slope. Mean EC50 values were calculated from the dose response replicates.  and the obtained mean EC50 values were multiplied with a protein-dependent correction factor (cf), resulting in the apparent Kd value (Kdapp). The correction factor is determined by calculating the ratio of the protein intensity of two consecutive pulldowns of the vehicle control sample2. Correction factors were set to the median of correction factors derived from 6 replicates (cfHDAC1=1, cfHDAC2=1, cfHDAC8=0.75, cfHDAC6=1, cfHDAC10=1, cfHDAC4=1, cfHDAC5=1, cfHDAC7=0.97, cfALDH11=0.89, cfALDH2=0.82, cfISOC1=0.85, cfISOC2=0.41, cfGATD3A=1, cfMBLAC2=0.78). Median correction factors equal to or larger than 1 indicate no relevant target depletion and were hence set to 1. Targets of the inhibitors were annotated manually. A protein was considered a target or interactor of a target if the resulting binding curve showed a sigmoidal curve shape with a dose dependent decrease of binding to the beads. Additionally, the number of unique peptides and MSMS counts per condition were taken into account.   1. Cox, J. et al. Accurate proteome-wide label-free quantification by delayed normalization and maximal peptide ratio extraction, termed MaxLFQ. Mol Cell Proteomics 13, 2513-2526 (2014). 2. Medard, G. et al. Optimized chemical proteomics assay for kinase inhibitor profiling. J Proteome Res 14, 1574-1586 (2015)."],"omics_type":["Proteomics"],"labhead":["Bernhard Kuster"],"instrument_platform":[""],"labhead_affiliation":["Chair of Proteomics and Bioanalytics, TUM School of Life Sciences, Technical University of Munich, Freising, Germany"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["severin.lechner@tum.de"],"publication":["36200994 Steimbach RR, Herbst-Gervasoni CJ, Lechner S, Stewart TM, Klinke G, Ridinger J, Géraldy MNE, Tihanyi G, Foley JR, Uhrig U, Kuster B, Poschet G, Casero RA, Médard G, Oehme I, Christianson DW, Gunkel N, Miller AK. Aza-SAHA Derivatives Are Selective Histone Deacetylase 10 Chemical Probes That Inhibit Polyamine Deacetylation and Phenocopy HDAC10 Knockout. J Am Chem Soc. 2022 144(41):18861-18875 10.1021/jacs.2c05030"],"submitter_affiliation":["Chair of proteomics and Bioanalytics, Technical Univerity Munich"],"submitter_country":["Germany"],"pubmed_abstract":["We report the first well-characterized selective chemical probe for histone deacetylase 10 (HDAC10) with unprecedented selectivity over other HDAC isozymes. HDAC10 deacetylates polyamines and has a distinct substrate specificity, making it unique among the 11 zinc-dependent HDAC hydrolases. Taking inspiration from HDAC10 polyamine substrates, we systematically inserted an amino group (\"aza-scan\") into the hexyl linker moiety of the approved drug Vorinostat (SAHA). This one-atom replacement (C→N) transformed SAHA from an unselective pan-HDAC inhibitor into a specific HDAC10 inhibitor. Optimization of the aza-SAHA structure yielded the HDAC10 chemical probe <b>DKFZ-748</b>, with potency and selectivity demonstrated by cellular and biochemical target engagement, as well as thermal shift assays. Cocrystal structures of our aza-SAHA derivatives with HDAC10 provide a structural rationale for potency, and chemoproteomic profiling confirmed exquisite cellular HDAC10-selectivity of <b>DKFZ-748</b> across the target landscape of HDAC drugs. Treatment of cells with <b>DKFZ-748</b>, followed by quantification of selected polyamines, validated for the first time the suspected cellular function of HDAC10 as a polyamine deacetylase. Finally, in a polyamine-limiting in vitro tumor model, <b>DKFZ-748</b> showed dose-dependent growth inhibition of HeLa cells. We expect <b>DKFZ-748</b> and related probes to enable further studies on the enigmatic biology of HDAC10 and acetylated polyamines in both physiological and pathological settings."],"pubmed_title":["Aza-SAHA Derivatives Are Selective Histone Deacetylase 10 Chemical Probes That Inhibit Polyamine Deacetylation and Phenocopy HDAC10 Knockout."],"pubmed_authors":["Steimbach Raphael R RR, Herbst-Gervasoni Corey J CJ, Lechner Severin S, Stewart Tracy Murray TM, Klinke Glynis G, Ridinger Johannes J, Géraldy Magalie N E MNE, Tihanyi Gergely G, Foley Jackson R JR, Uhrig Ulrike U, Kuster Bernhard B, Poschet Gernot G, Casero Robert A RA, Médard Guillaume G, Oehme Ina I, Christianson David W DW, Gunkel Nikolas N, Miller Aubry K AK"],"additional_accession":[]},"is_claimable":false,"name":"Aza-SAHA Derivatives are Selective Histone Deacetylase 10 Chemical Probes That Inhibit Polyamine Deacetylation","description":"We report the first selective chemical probes for histone deacetylase 10 (HDAC10) with unprecedented selectivity over other HDAC isozymes. HDAC10 deacetylates polyamines and has a distinct substrate specificity, making it unique among the 11 zinc-dependent HDAC hydrolases. Taking inspiration from HDAC10 polyamine substrates, we systematically inserted an amino group (“aza-scan”) into the hexyl linker moiety of the approved drug Vorinostat (SAHA). This one atom replacement (C-->N) transformed SAHA from an unselective pan-HDAC inhibitor into a specific HDAC10 inhibitor. Optimization of the aza-SAHA structure yielded DKFZ-748, which has a double-digit nanomolar IC50 against HDAC10 in cells and >500-fold selectivity over the closest relative HDAC6 as well as the Class I enzymes (HDAC1, 2, 3, 8). The selectivity over other class I, IIb, IIa HDACs and common the off-targets MBLAC2, ISOC1/2, GATD3Aand ALDH2 was confirmed via chemotproteomic selecitivty profiling. Potency of our aza-SAHA derivatives is rationalized with HDAC10 co-crystal structures and demonstrated by cellular and biochemical target-engagement, as well as thermal-shift, assays. Treatment of cells with DKFZ-748, followed by quantification of selected polyamines, confirmed for the first time the suspected cellular function of HDAC10 as a poly-amine deacetylase. Selective HDAC10 chemical probes provide a valuable pharmacological tool for target validation and will enable further studies on the enigmatic biology of HDAC10 and acetylated polyamines. HDAC10-selective aza-SAHA derivatives are not cytotoxic, which opens the doors to novel therapeutic applications as immunomodulators or in combination cancer therapy.","dates":{"publication":"2026-06-02","submission":"2022-03-20"},"accession":"PXD032671","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2737160","NEWT:2042546","NEWT:148942","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:89187","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:57577","NEWT:156563","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:44270","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:93217","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:82569","NEWT:661410","NEWT:488003","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:2433","NEWT:3767","NEWT:433727","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:1176302","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:44250","NEWT:77151","NEWT:317447","NEWT:698761","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:11308","NEWT:12637","NEWT:2164133","NEWT:1180","NEWT:2767846","NEWT:1343074","NEWT:314344","NEWT:108061","NEWT:143292","NEWT:224308","NEWT:3134131","NEWT:49928","NEWT:160621","NEWT:110368","NCBITaxon:5204","NEWT:1916073","NEWT:1303873","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:160620","NCBITaxon:77643","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1410384","NEWT:1310173","NEWT:1072569","NEWT:1072568","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:135666","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1336794","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3710","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:65121","NEWT:3716","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:118221","NEWT:34869","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:550537","NEWT:284812","NEWT:284811","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:34875","NEWT:10882","NEWT:1431297","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:1423687","NEWT:657322","NEWT:10886","NEWT:3707","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:1301262","NEWT:319224","NEWT:2305479","NEWT:215451","NEWT:460519","NEWT:272843","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:223074","NEWT:2499525","NEWT:467144","NEWT:142786","NEWT:28196","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:387344","NEWT:657318","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:272831","NEWT:987059","NEWT:491","NEWT:422203","NEWT:460523","NEWT:2422","NEWT:2423","NEWT:3755","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","NEWT:1195466","NEWT:85698","NEWT:291146","NEWT:233271","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:34839","NEWT:476","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NEWT:106299","NCBITaxon:50557","NEWT:63363","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:714485","NEWT:445","NEWT:2003758","NEWT:29486","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:1120755","NEWT:1862567","NEWT:591090","NEWT:30455","NEWT:28141","NEWT:9030","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:1325292","NEWT:219798","NEWT:548","NEWT:150475","NEWT:546","NEWT:1431340","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:451515","NEWT:8673","NEWT:550","NEWT:10804","NEWT:52694","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:40686","NEWT:1225786","NEWT:366497","NEWT:771870","NEWT:8665","NEWT:51338","NEWT:771875","NEWT:377142","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:311339","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:2585209","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:536","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:51315","NEWT:52641","NEWT:353152","NEWT:116597","NEWT:353153","NEWT:116598","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:6055","NEWT:13037","NEWT:518","NEWT:519","NEWT:941638","NEWT:511","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:13064","NEWT:529120","NEWT:7375","NEWT:300641","NEWT:39655","NEWT:38323","NEWT:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:6039","NEWT:37003","NEWT:1045775","NE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