{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD060264/9_SPROX.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD060264/12_SPROX.msf"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD060264/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD060264/9_Enriched3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD060264/12_NE.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD060264/9_Enriched1_20230929191647.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD060264/9_NE.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD060264/12_Enriched1_20230929164316.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD060264/12_Enriched3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD060264/9_Enriched2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD060264/12_Enriched2.raw"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["michael.c.fitzgerald@duke.edu"],"submitter":["Natalie Labbe"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Rna","Proteomics","Sprox"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD060264"],"sample_protocol":["12-bp G3 RNA was first annealed in 150 mM KCl using 5-minute heat treatment at 95 ◦C, followed by cooling on ice for 10 minutes. The SPROX treatments were prepared in a total volume of 130 µL and included 60 U of RNase Inhibitor, 1% DMSO, 14.1 µM RNA (or equivalent volume of 150 mM KCl, vehicle control), 150 µM DMZ-P8/DMZ-P13 for the small molecule treated samples (diluted from 1.5 mM stocks, 100% DMSO), and 3 mg/mL LNCaP nuclear lysate and made to volume with phosphate buffered saline (Corning). All six treatments were 1) lysate (L) only (DMSO + vehicle), 2) G3 (DMSO + G3), 3) G3 + DMZ-P8 (DMZ-P8 + G3), 4) G3 + DMZ-P13 (DMZ-P13 + G3), 5) DMZ-P8 (DMZ-P8 + vehicle) and 6) DMZ-P13 (DMZ-P13 + vehicle). After treatments were prepared in biological triplicate, the samples were allowed to rotate at 4 ◦C for 1.5 hours prior to running the SPROX protocol. These treated samples were evaluated in SPROX experiments performed in biological triplicate using a one-pot SPROX method.76 In short, for each treatment replicate 360 µg of total protein was equally distributed across a series of 12 buffers containing 20 mM phosphate (pH 7.4), 150 mM NaCl, and final urea denaturant concentrations equally spaced in 0.5 M intervals from 0 to 5.5 M. The aliquoted treatments were diluted three-fold in the urea buffers and equilibrated for 2 hours at room temperature, at a final equilibration sample concentration of 4.7 µM G3, 20 U of RNase inhibitor, 0.33% DMSO, 50 µM DMZ-P8/DMZ-P13, 1 mg/mL LNCaP nuclear lysate, 20 mM phosphate pH 7.4, 150 mM NaCl, and desired urea con-centrations. A methionine oxidation reaction was performed in each denaturant-containing sample through the addition of 3 µL of 30% (v/v) H2O2. The final protein and H2O2 concentration in each denaturant-containing tube was 1 mg/mL and 0.9 M, respectively. The methionine oxidation reaction was allowed to proceed for 3 minutes before it was quenched with 250 µL of 1 M TCEP. Equal aliquots of the denaturant-containing protein samples in the denaturant series were combined in one tube. This was done for each of the 6 treatment conditions as well as 3 biological replicates for each treatment (6 total replicates of lysate control were prepared for two mass spectrometry experiments). The resulting 12 (treatments 1-4 for Ex-periment A) and 9 (treatments 1, 5-6 for Experiment B) protein samples were then prepared for LC-MS/MS quantitative bottom-up proteomic analysis using using an isobaric mass tagging strategy involving 12 and 9 channels from a TMTpro 16-plex for Experiments A and B (respectively) and a previously described iFASP protocol.77 The methionine-containing peptides in the samples were enriched using a Pi3 methionine reagent kit following the manufacturer’s protocol (Nest Group). A C18 Macrospin column was used to desalt the labeled protein sample, which was ultimately subjected to triplicate LC-MS/MS analyses."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["LC-MS/MS analyses of the samples generated in the SPROX experiments were performed on a Thermo Orbitrap Exploris mass spectrometer 480 system interfaced with a ThermoEasy nano LC 1200. A total of 1 µg of total peptide dissolved in 0.1% trifluoroacetic acid, and 2% acetonitrile in HPLC grade water to give a final concentration of 1 mg/mL was injected onto the column and subjected to an LC-MS/MS analysis using a nanoViper 2Pk C18, 3 µm, 100 Å, 75 µm X 25 cm analyt-ical column (ThermoFisher) and gradient elution using a 90-minute linear gradient of 4 – 35% acetonitrile at a flow rate of 400 nL/min. The analytical column was maintained at a temperature of 45 ◦C. A data-dependent acquisition was set up using a cycle time of 2.5 s. The resolution of the MS1 and MS2 data were at 120k and 45k, respectively. A normalized AGC target of 300% was used for both MS1 and MS2 analyses. The collision energy was set to 36% with an MS1 scan range of 375 – 1500 m/z, and an isolation window of 1.2 m/z with a dynamic exclusion duration of 45 s. Each peptide sample was analyzed in triplicate by LC-MS/MS (three biological replicates run in triplicate for each experiment). The raw data from the LC-MS/MS experiments were searched against the 2017-10-25 release of the Uniprot Knowledge-base mammalian proteome using Proteome Discoverer 2.3 (ThermoFisher) and the SEQUEST HT database search algo-rithm"],"omics_type":["Proteomics"],"labhead":["Michael C. Fitzgerald"],"instrument_platform":[""],"labhead_affiliation":["Chemistry, Duke University, USA"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["natalie.labbe@duke.edu"],"publication":["Not available"],"submitter_affiliation":["Duke University Department of Chemistry"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Small molecules reveal differential shifts in stability and protein binding for G-quadruplex RNA","description":"The potential of therapeutically targeting RNA with small molecules continues to grow yet progress is hindered by difficulties in determining specific mechanisms of action, including impacts on RNA-protein binding. RNA G-quadruplexes (rGQs) are a particularly promising target due to their range of biological functions, structural stability, and hydrophobic surfaces, which promote small molecule and protein interactions alike. Challenges arise due to 1) the low structural diversity among rGQs, thereby limiting binding selectivity, and 2) a lack of knowledge regarding how small molecules can manipulate rGQ-protein binding on a global scale. We first leveraged a small molecule library privileged for RNA tertiary structures that displayed differential binding to rGQs based on loop length, consistent with computational predictions for DNA GQs. We next utilized an RT-qPCR-based assay to measure stability against enzymatic readthrough, expected to be a common mechanism in rGQ function. We discovered small molecules with significant, bidirectional impacts on rGQ stability, even within the same scaffold. Using Stability of Proteins from Rates of Oxidation (SPROX), a stability-based proteomics method, we then eluci-dated proteome level impacts of both stabilizing and destabilizing rGQ-targeting molecules on rGQ-protein interactions. This technique revealed small molecule-induced impacts on a unique subset of rGQ-binding proteins, along with proteins that exhibited differential changes based on the identity of the small molecule. The domain and peptide-level insights resulting from SPROX allow for the generation of specific hypotheses for both rGQ function and small molecule modulation thereof. Taken altogether, this methodology helps bridge the gap between small molecule-RNA targeting and RNA-protein interac-tions, providing insight into how small molecules can influence protein binding partners through modulation of target RNA structures.","dates":{"publication":"2026-06-23","submission":"2025-01-27"},"accession":"PXD060264","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: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","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: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:111225","NEWT:7719","NEWT:5530","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:49928","NEWT:3349","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:55350","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: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: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:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2709072","NEWT:2499525","NEWT:2853422","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:108458","NEWT:5936","NEWT:321967","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:415978","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","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:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","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: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:33941","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:575412","NEWT:28112","NEWT:49012","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:130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