{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070051/checksum.txt"],"Csv":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070051/241216_GCN5_0uM_pos02_0sec_03_IA_final_peptide.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070051/241216_GCN5_0uM_pos02_0sec_01_IA_final_peptide.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070051/241216_GCN5_0uM_pos02_0sec_02_IA_final_peptide.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070051/240208_GCN5_ND_20ug_IA_final_peptide.csv"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070051/GCN5_4250_Kd_300s.hdx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070051/GCN5_4250H.hdx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070051/GCN5_4250_Kd_3000s.hdx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070051/JASMS_raw_data.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070051/GCN5_4250_Kd_30s.hdx"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["gmasson001@dundee.ac.uk"],"submitter":["Glenn Masson"],"technology_type":["Data-dependent acquisition","HDMSE","Mass Spectrometry"],"software":["Not available"],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070051"],"sample_protocol":["Prior to deuterium incorporation experiment, a protein sequence coverage map was first achieved by analysing undeuterated PfGCN5 protein in the following condition: 60 µL of the 1 µM protein in 20 mM HEPES pH 7.5, 150 mM NaCl, 0.5 mM TCEP and 1% DMSO was mixed with to 50 µL ice-cold quenched buffer (4M Urea containing 2% formic acid (FA)).  Stocks (PfGCN5 20 µM or PfGCN5 20 µM + small molecule 100 µM) were prepared in 20 mM HEPES pH 7.5, 150 mM NaCl, 0.5 mM TCEP and 1% DMSO (v/v) and stored at 0.1 ºC. HDX labelling was performed at 0, 30, 300 and 3000 seconds; 3 µL of sample stock was mixed with 57 µL of D2O buffer (20 mM HEPES pH 7.5, 150 mM NaCl, 0.5 mM TCEP and 1% DMSO in 94% D2O) at 20 ºC resulting in 89.4% D2O (v/v) during labelling. D2O buffer was supplemented with 100 µM small molecule DDD0244420. After the HDX reaction, 50 µL of the labelled sample was mixed with 50 µL quench buffer (4M Urea containing 2% FA) at 0.1 ºC for 1 min prior to LCMS data acquisition. For the 0.005 min time point, the samples were prepared on ice in a 4 ºC room with pre-chilled D2O buffer and pipette tips and incubated with D2O buffer for 3 seconds. For 0.05 min time point, the samples were prepared and incubated with D2O buffer for 3 seconds at room temperature. Samples were frozen immediately into liquid nitrogen and later stored at -80 ºC until further analysis. All deuterium-labelled samples were repeated three times.  For Protein-ligand affinity determination, HDX reaction were conducted by diluting 3 µL of the 20 µM protein sample in the absence or presence of a given small molecule at the serious concentrations with 57 µL of the D2O buffer and allowed to exchange for 5 min at 20 ºC. 50 µL of the labelled sample was mixed with 50 µL quench buffer (4M Urea containing 2% FA) at 0.1 ºC for 1 min prior to LCMS data acquisition."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["HDX-MS Data were acquired using the HDX manager (Waters Corps) set at 0.1 ºC in-line with a SELECT SERIES Cyclic IMS QTOF instrument (Waters Corps). Liquid handling was performed using a PAL3 robotic Tool change system and Chronos Software (Leap Technologies). In-line digestion was conducted using an enzymate BEH Pepsin 2.1x30mm Column (Waters, Corps) at 20 ºC, where protein was digested for 2 min. Peptides were desalted by ACQUITY UPLC BEH C18 1.7 um, 5 mm x 2.1mm VanGuard Precolumn (Waters, Corps) before eluted onto a reverse-phase separation ACQUITY UPLC 1.7 um particle, 100 mm x 1mm C18 column (Waters, Waters Corps.) in buffer A (water with 0.1% formic acid) with a 12 min 5-85% gradient of buffer B (100% acetonitrile with 0.1% formic acid). Data were acquired over a mass range of 50-1200 m/z with a spray voltage of 2.0 kV. Peptide identification was performed using the ProteinLynx Global Serve (PLGS3.0.3 Waters Corps). Data from three samples of non-deuterated PfGCN5 collected in HDMSe mode was used for the peptide sequence identification. All comparative experiments were performed under identical experimental conditions.   Raw data were imported into HDExaminer 3.5.0 (Sierra Analytics) or Newmarket (unreleased software, Waters Corps) for HDX analysis. Deuterium incorporation was not corrected for back-exchange and is therefore reported as relative."],"omics_type":["Proteomics"],"labhead":["Glenn Masson"],"instrument_platform":[""],"labhead_affiliation":["University of Dundee"],"submission_type":["PARTIAL"],"species":["Plasmodium Falciparum 58.1"],"submitter_mail":["gmasson001@dundee.ac.uk"],"publication":["41915381 Lin, Magalhaes LG, McMillan J, Eadsforth TC, Stewart G, Cartmill KR, Postis VLG, Masson GR. Residue-Level Determination of Small-Molecule-Protein Affinities by Hydrogen-Deuterium Exchange Mass Spectrometry. J Am Soc Mass Spectrom. 2026 10.1021/jasms.6c00020"],"submitter_affiliation":["University of Dundee"],"submitter_country":["United Kingdom"],"pubmed_abstract":["Hydrogen-Deuterium Exchange Mass Spectrometry (HDX-MS) is an established tool in drug discovery, used to characterize target engagement and conformational dynamics, and frequently used in both biopharmaceutical and small molecule drug discovery. Conventional HDX-MS experiments are performed at saturating ligand concentrations to generate a binding \"footprint\", where decreased solvent exchange reflects a local structural stabilization or reduced solvent accessibility upon binding. Here, we present an extended HDX-MS and HDX-MS/MS titration workflow with electron capture dissociation (ECD) fragmentation capable of estimating apparent dissociation constants (<i>K</i><sub>D</sub><sup>app</sup>) at global, peptide, and single amino acid resolution by fitting uptake-concentration relationships under EX2 exchange and Langmuir binding assumptions. The ability to determine affinity constants in a spatially resolved manner combined with the automation available in HDX-MS sample handling and data analysis enables quantitative mapping of ligand-protein interactions and provides a scalable approach for structure-activity relationship studies in drug discovery."],"pubmed_title":["Residue-Level Determination of Small-Molecule-Protein Affinities by Hydrogen-Deuterium Exchange Mass Spectrometry."],"pubmed_authors":["Lin De, Magalhaes Luma Godoy LG, McMillan Joel J, Eadsforth Thomas C TC, Stewart Greg G, Cartmill Kieran R KR, Postis Vincent L G VLG, Masson Glenn R GR"],"additional_accession":[]},"is_claimable":false,"name":"Determination of highly accurate small molecule:protein affinity constants at amino acid resolution using Hydrogen Deuterium Exchange Mass Spectrometry (HDX-MS)","description":"Hydrogen Deuterium Exchange Mass Spectrometry (HDX-MS) has been widely adopted as part of the drug development pipeline, frequently used in both the development of biopharmaceuticals and small molecule compound development to assess target engagement spatially. Frequently, HDX-MS analyses are conducted at saturating compound concentrations to produce a compound binding “footprint” where typically the reductions in solvent exchange associated with compound engagement can be interpreted as evidence of a localized hydrogen bond network disruption caused by a binding event. Here we present a workflow of compound titration in both HDX-MS and HDX-MS/MS workflows using ECD to determine compound dissociation constants at a global, peptide and single amino acid resolution. The ability to determine affinity constants in a spatially resolved manner using the automation available to HDX-MS sample production and data analysis is likely to have applications in drug discovery and medicinal chemistry.","dates":{"publication":"2026-04-01","submission":"2025-10-29"},"accession":"PXD070051","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","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:294671","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:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:3357","NEWT:7719","NEWT:29073","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:2020713","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:2502409","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:342808","NEWT:2579791","NEWT:44685","NEWT:161934","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:3715","NEWT:2065263","NEWT:199225","NEWT:177437","NEWT:717966","NEWT:10891","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: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:10886","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:1955249","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:485","NEWT:56636","NEWT:2499525","NEWT:1122981","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:1502","NEWT:128017","NEWT:2836","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:119562","NEWT:1883446","NEWT:31345","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:235455","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:717989","NEWT:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166314","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:1871049","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:51350","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:253237","NEWT:10804","NEWT:33941","NEWT:554","NEWT:451516","NEWT:552",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