Prideapplication/xmlftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/modificationSpecificPeptides_PRIDE.txtftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/experimental_design_PRIDE.txtftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/checksum.txtftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231017_NeoPhore_Cysteinome_TMT_F14.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231009_NeoPhore_cysteinome_DMSO_4_PRM.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231017_NeoPhore_Cysteinome_TMT_F9.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231009_NeoPhore_cysteinome_DMSO_5_PRM.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231017_NeoPhore_Cysteinome_TMT_F5.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231009_NeoPhore_cysteinome_DMSO_3_PRM.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231009_NeoPhore_cysteinome_DMSO_2_PRM.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231017_NeoPhore_Cysteinome_TMT_F8.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231017_NeoPhore_Cysteinome_TMT_F13.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231009_NeoPhore_cysteinome_0p5uM_4_PRM.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231017_NeoPhore_Cysteinome_TMT_F4.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231009_NeoPhore_cysteinome_0p5uM_3_PRM.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231009_NeoPhore_cysteinome_0p5uM_2_PRM.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231017_NeoPhore_Cysteinome_TMT_F3.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231009_NeoPhore_cysteinome_0p5uM_1_PRM.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231017_NeoPhore_Cysteinome_TMT_F7.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231017_NeoPhore_Cysteinome_TMT_F16.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231017_NeoPhore_Cysteinome_TMT_F12.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231009_NeoPhore_cysteinome_0p5uM_5_PRM.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231017_NeoPhore_Cysteinome_TMT_F2.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231017_NeoPhore_Cysteinome_TMT_F15.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231009_NeoPhore_cysteinome_3uM_5_PRM.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231009_NeoPhore_cysteinome_DMSO_1_PRM.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231017_NeoPhore_Cysteinome_TMT_F6.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231017_NeoPhore_Cysteinome_TMT_F11.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231009_NeoPhore_cysteinome_3uM_4_PRM.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231017_NeoPhore_Cysteinome_TMT_F1.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231009_NeoPhore_cysteinome_3uM_1_PRM.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231017_NeoPhore_Cysteinome_TMT_F10.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231009_NeoPhore_cysteinome_3uM_3_PRM.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077673/20231009_NeoPhore_cysteinome_3uM_2_PRM.rawprimaryOK200rob.howes@crl.comAlexia HervieuData-dependent acquisitionMass SpectrometryBottom-up proteomicsColon Cancerhttps://www.ebi.ac.uk/pride/archive/projects/PXD077673Permanent Cell Line CellCell CultureSW620 cells treated with NP1867 at 0.5 and 3 uM, or vehicle control DMSO, for 2 hours were pelleted, washed with PBS and lysed in 5% SDS in 50 mM TEAB containing protease inhibitors and nuclease. The lysates were clarified by centrifugation at 15,000 xg for 10 min at room temperature. Protein concentration was measured using a BCA assay. 120 µg of total protein was prepared at 1 µg/μL and treated with IA-DTB (10 mM in anhydrous DMSO) to give a final concentration of 100 μM and shaken in the dark for 1 h at room temperature. Samples were cleaned-up using methanol-chloroform precipitation by adding 480 μL cold methanol, 120 μL chloroform and 360 μL of water followed by vortexing. Proteins were precipitated by centrifugation at 10,000 xg for 10 min at 4°C. Upper and lower layers were removed, and 1 mL methanol was added to the pellets. Samples were subsequently vortexed and centrifuged at 16,000 xg for 10 min at 4°C. The protein pellets were air dried, resolubilised in buffer (90 µL 8 M urea, 10 mM dithiothreitol, 50 mM TEAB), incubated at 37°C for 30 min, and then incubated with 10 µL 0.5M iodoacetamide for 20 min in dark. 16.6 µL (20 µg) of sample mixture was withdrawn for targeted proteomics analysis (See: Sample preparation for PMS2 Cys73 target engagement study by mass spectrometry analysis). The remaining sample was diluted with 300 µL 50 mM TEAB and 2µg trypsin was added for overnight digestion at 37°C. The IA-DTB labelled peptides were enriched by incubating samples with streptavidin beads (Dynabeads Streptavidin MyOne C1, ThermoFisher Scientific), pre-washed in enrichment buffer (50 mM TEAB, pH 8.5, 150 mM NaCl, 0.2% IGEPAL CA-630), for 3 h at room temperature on a rotating wheel. Beads were washed 2x in 500 µL wash buffer (50 mM TEAB, pH 8.5, 150 mM NaCl, 0.1% IGEPAL CA-630), 3x in 50mM TEAB and 3x in water. Peptides were eluted from the beads 3x in 250 μL 50% acetonitrile/0.1% (v/v) formic acid and dried by vacuum centrifugation. The peptide samples were resolubilized in 100 µL 50 mM TEAB with sonication and were TMT labelled according to the manufacturer’s instructions (TMTpro 16plex). Samples were pooled, dried by vacuum centrifugation, resuspended in 40 µL water and fractionated using high pH reverse phase on an Agilent 1100 series off-line high pH LC system. Peptides were separated on an Agilent Zorbax RR Extend-C18 column (3.0 x 150 mm, 3.5 µm, 80Å) at a flow rate of 0.5 mL/min with buffer A (20 mM NH4OH in water) and buffer B (20 mM NH4OH in 90% acetonitrile) using following gradient: 5–37% buffer B over 41 min, 37 to 90% buffer B over 2 min; column wash with 90% buffer B and re-equilibration to 5% buffer B to complete the 60 min run. The fractions were dried by vacuum centrifugation. Samples were resuspended in 50 µL 0.1% formic acid, sonicated for 10 min, and spun down at 16,100 x g for 5 min. 20 μL of sample was injected for discovery LC-MS analysis.PrideNot availableMass spectrometry (LC-MS) analysis: Peptide samples were analysed on an Orbitrap ExplorisTM 240 mass spectrometer, coupled in-line to a Dionex UltimateTM 3000 RSLCnano system (ThermoFisher Scientific). The nanoLC method was set up with buffer A as 0.1% (v/v) formic acid in water and buffer B as 0.1% (v/v) formic acid in 100% (v/v) acetonitrile. The mobile phase for loading was 0.1% (v/v) formic acid in water. Peptides were loaded onto a pre-column (ThermoFisher Scientific Acclaim™ PepMap™ 100 C18, 5 µm particle size, 100 Å pore size, 0.1 mm i.d. x 20 mm length) and separated on an analytical column (ThermoFisher Scientific EASY-Spray™ PepMap™ RSLC C18, 2 µm particle size, 100 Å pore size, 75 μm i.d. x 500 mm length) at a flow rate of 250 nL/min. For discovery LC-MS, the samples were run in data-dependent acquisition mode and were separated following the gradient: of 2 - 37% buffer B over 69 min, followed by 37 - 80% buffer B over 1 min; at the end the column was washed with 80% buffer B and re-equilibrated to 2% buffer B to complete the 90 min run. The Orbitrap Exploris 240 equipped with FAIMS pro (-45 V and -60 V) was operated in positive-ion data-dependent mode. Precursor ion (MS1) scans were performed in the Orbitrap mass analyzer in the range of 350–1,400 m/z, with a resolution of 120,000 (at 200 m/z). Precursor ions were isolated using a quadrupole mass filter with an isolation width of 0.7 m/z and fragmented using higher energy collision dissociation (HCD) with a collision energy of 30%. MS/MS fragment ions were analysed in the Orbitrap mass analyser with a resolution of 60,000 (at 200 m/z). For PMS2 target engagement studies, the peptide samples were run in parallel reaction monitoring (PRM)-based targeted LC-MS and were separated in following gradient: 5 - 37% buffer B over 42 min, followed by 37 - 80% buffer B for 1 min; at the end the column was washed with 80% buffer B and re-equilibrated to 2% buffer B to complete the 65 min run. The survey scan (MS1) scans were performed in the Orbitrap mass analyzer at resolution of 30,000 (at 200 m/z), max injection time 50 ms and AGC target at 300%. Precursor ions were isolated using a quadrupole mass filter with an isolation width of 0.7 m/z and fragmented using higher energy collision dissociation (HCD) with a collision energy of 30%. Targeted MS2 scan in which the m/z ratios for several peptides were monitored in the 2+ charge state with an isolation width of 1.2 m/z and fragmented using higher energy collision dissociation (HCD) with a collision energy of 30%. Peptide sequence, m/z, Orbitrap resolution, max ion injection time (IIT) and AGC target are shown in Supplementary Table 3. Data analysis. For targeted PRM target engagement, raw mass spectrometry files from PRM-based LC-MS were processed and analysed using Skyline12. Area-under-curve abundance values, normalised to total ion current, for compound-treated samples were compared to vehicle-treated control samples; decreased abundance of carbamidomethylated Cys73-containing PMS2 peptide was inferred as resulting from Cys73 adduction by NP1867. For reactive cysteinome profiling, data were analysed in MaxQuant (version 2.2.0.0) with IA-DTB as fixed and carbamidomethylation as variable modification. The data were normalised using global median normalisation. Differential abundance analysis was done using Limma pairwise moderated t-testing (RStudio) with 3 or more values present for quantitation.ProteomicsRob Howes,PARTIALDiscovery | Charles River Chesterford Research Park, CB10 1XL, United Kingdom P: +44 1799 533 500Homo Sapiens (human)42013405 Blagg J, Riou P, Hervieu A, Piumatti E, Rodriguez-Plata MT, Battuello P, Peall A, Amodio V, Vitiello PP, Nightingale DJH, Bago R, Tongue P, Slater T, Parmar K, Patel P, Rodríguez González J, Clark DE, Langley GW, Nichols C, Guarne A, Winship PCM, Baker M, Drysdale M, Germano G, Bardelli A. Pharmacological inhibition of PMS2 induces MMR deficiency and response to immune checkpoint blockade. Cancer Discov. 2026 10.1158/2159-8290.cd-26-0003alexia.hervieu@neophore.comNeoPhore Ltd.United KingdomDNA mismatch repair (MMR) detects and corrects post-replicative DNA alterations; it is deregulated in up to 20% of human cancers. MMR-deficient (MMR-d) cancers display increased tumour mutational burden (TMB), microsatellite instability (MSI) and are eligible for checkpoint inhibitor (CPI) immunotherapy which commonly elicits durable responses. We reasoned that pharmacological blockade of MMR could broaden the patient population eligible for immunotherapy. Here we reveal MMR protein PMS2 as a druggable target and describe the discovery and characterisation of first-in-class small molecule MMR pathway modulator NP1867. In vitro treatment of murine cancer cells abrogates MMR function and elicits an MMR-d genotype including increased TMB, MMR-d mutational signatures, and MSI-High (MSI- H) status. Inoculation of syngeneic immunocompetent mice with cancer cells pretreated with NP1867 leads to CPI sensitivity, tumour growth delay, and complete responses. For the first time, we demonstrate pharmacological targeting of MMR to proactively rewire the tumour-host relationship for therapeutic purposes.Pharmacological inhibition of PMS2 induces MMR deficiency and response to immune checkpoint blockade.Blagg Julian J, Riou Philippe P, Hervieu Alexia A, Piumatti Eleonora E, Rodriguez-Plata Maria T MT, Battuello Paolo P, Peall Adam A, Amodio Vito V, Vitiello Pietro Paolo PP, Nightingale Daniel J H DJH, Bago Ruzica R, Tongue Paige P, Slater Tessa T, Parmar Kalpesh K, Patel Pradip P, Rodríguez González Javier J, Clark David E DE, Langley Gareth W GW, Nichols Charles C, Guarne Alba A, Winship Paul C M PCM, Baker Matthew M, Drysdale Martin M, Germano Giovanni G, Bardelli Alberto AfalsePMS2 inhibitor NP1867 cysteinome adduction by cell-based proteomincsMMR protein PMS2 is a druggable target. Discovery and characterisation of first-in-class small molecule MMR pathway modulator NP1867.2026-04-282026-04-27PXD077673NEWT:3555NEWT:71647NEWT:330879NEWT:260201NEWT:35554NCBITaxon:12939NEWT:377960NEWT:32046NEWT:544496NEWT:59529NEWT:2042546NEWT:32049NEWT:1392696NEWT:259447NEWT:295546NEWT:45351NEWT:445974NEWT:43179NEWT:180454NEWT:5722NCBITaxon:1280NEWT:112503NEWT:1129NEWT:309807NEWT:10245NEWT:55153NEWT:59753NEWT:89184NEWT:309800NEWT:281395NEWT:1211601NEWT:876138NEWT:44271NEWT:193516NEWT:351581NEWT:43186NEWT:428146NEWT:1117NEWT:498257NEWT:10036NEWT:1590NEWT:498019NEWT:1351NEWT:1438992NEWT:1352NEWT:2649997NEWT:1147161NEWT:661410NEWT:638632NEWT:43150NEWT:263737NEWT:224326NEWT:1333499NEWT:376619NCBITaxon:79857NEWT:1096976NEWT:5702NEWT:95648NEWT:1589NEWT:135622NEWT:1349NEWT:35786NEWT:1580NEWT:399784NEWT:96731NEWT:383379NEWT:1401257NEWT:418106NEWT:10029NEWT:913645NEWT:44491NEWT:641809NEWT:27933NEWT:556484NEWT:317447NEWT:4688NEWT:7955NEWT:7719NEWT:7959NEWT:2261NEWT:868565NEWT:135674NEWT:94323NEWT:31156NEWT:3112NEWT:79329NEWT:4442NEWT:192875NEWT:30069NEWT:12637NEWT:59729NEWT:2164133NEWT:284218NEWT:295105NEWT:108061NEWT:60711NEWT:1316931NEWT:224308NEWT:3347NEWT:511145NEWT:160621NEWT:212790NEWT:931281NEWT:4432NEWT:5762NEWT:5763NEWT:658457NEWT:1310161NEWT:77133NEWT:295358NEWT:145481NEWT:1310165NEWT:29058NCBITaxon:79824NEWT:2246NEWT:2652724NEWT:5757NEWT:68415NCBITaxon:4563NEWT:5755NEWT:44688NEWT:44689NEWT:44447NEWT:752555NEWT:498211NEWT:5759NEWT:347256NEWT:1736231NEWT:5518NEWT:398007NEWT:1527468NEWT:1392NEWT:498217NEWT:498216NEWT:2242NEWT:11320NEWT:286NEWT:391619NEWT:246196NEWT:287NEWT:246197NEWT:145458NEWT:633149NEWT:1149786NEWT:10239NEWT:68895NEWT:44685NEWT:161934NEWT:4897NEWT:1148NEWT:5744NEWT:72901NEWT:213863NEWT:5508NEWT:3329NEWT:5507NEWT:410661NEWT:55571NEWT:35500NEWT:1140NCBITaxon:2157NEWT:1143NEWT:4896NEWT:1262161NEWT:1314781NEWT:1287689NEWT:1390NEWT:11557NEWT:1094343NEWT:1462472NEWT:1336795NEWT:644042NEWT:294NEWT:1773NEWT:1182590NEWT:3712NEWT:82380NEWT:3711NEWT:935293NEWT:375146NEWT:2065263NEWT:177437NEWT:1772NEWT:10418NEWT:118698NEWT:1616117NEWT:263NEWT:118696NEWT:34865NEWT:52283NEWT:11988NEWT:284812NEWT:8175NEWT:400667NEWT:43330NEWT:1603293NEWT:408169NEWT:44664NEWT:47946NEWT:3702NEWT:1245466NEWT:244366NEWT:243277NEWT:1246791NEWT:7067NEWT:118694NEWT:586722NEWT:2850NEWT:118691NEWT:34871NEWT:33548NEWT:274NEWT:7070NCBITaxon:287NEWT:408172NEWT:408170NEWT:96794NEWT:3708NEWT:332648NEWT:44670NEWT:536231NEWT:376219NEWT:219813NEWT:1510NEWT:1436733NEWT:460519NEWT:1247411NEWT:1515NEWT:572307NEWT:1432138NEWT:9238NEWT:1424507NEWT:1194599NEWT:272844NEWT:1303443NEWT:333760NEWT:485NEWT:34607NEWT:56636NEWT:1513458NEWT:1233681NCBITaxon:40559NEWT:506599NEWT:2853422NEWT:81077NEWT:84588NEWT:1679718NEWT:480NEWT:65349NEWT:67767NEWT:46835NEWT:109757NEWT:582580NEWT:300852NEWT:1502NEWT:128017NEWT:376686NEWT:95486NEWT:508771NEWT:1121405NEWT:1883446NEWT:253NCBITaxon:2759NEWT:1233435NEWT:93061NEWT:93062NEWT:34613NCBITaxon:4932NEWT:1748NEWT:109760NEWT:29031NEWT:108673NEWT:943274NEWT:644223NEWT:1263082NEWT:235443NEWT:108458NEWT:5936NEWT:272623NEWT:272624NEWT:320637NEWT:886559NEWT:3750NEWT:55521NEWT:983964NEWT:118499NEWT:11706NEWT:32644NEWT:527796NEWT:1130798NEWT:55529NEWT:499175NEWT:109779NEWT:3745NEWT:1715989NCBITaxon:4751NEWT:476272NEWT:3747NEWT:195051NEWT:3988NEWT:1116234NEWT:561007NEWT:1255228NEWT:649908NEWT:410289NEWT:373153NEWT:3983NEWT:203696NEWT:472NEWT:352472NEWT:97441NEWT:1154756NEWT:1071661NEWT:1202531NEWT:1202532NEWT:360094NEWT:1408223NEWT:470NEWT:1408224NEWT:41364NEWT:5911NEWT:1313NEWT:1218097NEWT:1080348NCBITaxon:50557NEWT:1314NEWT:39251NEWT:39491NEWT:212142NCBITaxon:5811NEWT:29491NEWT:101841NEWT:446NEWT:153481NEWT:2014887NEWT:1499105NEWT:33952NEWT:445NEWT:153009NEWT:261756NEWT:571256NEWT:40483NEWT:63366NEWT:63367NEWT:688333NEWT:215402NCBITaxon:548681NEWT:318586NCBITaxon:5820NEWT:1547NEWT:272634NEWT:198107NEWT:1979401NEWT:9031NEWT:27292NEWT:1872122NEWT:1308NEWT:7091NEWT:1034015NEWT:760568NEWT:141262NEWT:108931NEWT:1293497NEWT:1055524NEWT:1813NEWT:4087NEWT:9778NEWT:306NEWT:150475NEWT:303NEWT:267872NEWT:97477NEWT:7111NEWT:347515NEWT:172269NEWT:9534NEWT:6269NEWT:5180NEWT:256737NEWT:4090NEWT:4092NEWT:9541NEWT:8694NEWT:4093NEWT:33936NEWT:4096NEWT:8692NEWT:2903NEWT:185579NEWT:941442NEWT:536088NEWT:13076NEWT:1226408NEWT:7108NEWT:40479NEWT:43989NEWT:4076NEWT:142615NEWT:317NEWT:1006581NEWT:33940NEWT:885318NEWT:39488NEWT:550NEWT:4081NEWT:273068NEWT:554NEWT:98334NEWT:451516NEWT:552NEWT:231663NEWT:4084NEWT:1325291NEWT:63577NEWT:36185NEWT:1054211NEWT:1225786NEWT:7574NEWT:1715256NEWT:30640NEWT:575412NEWT:929793NEWT:1507179NEWT:29204NEWT:28112NEWT:114155NEWT:6493NEWT:6494NEWT:6491NEWT:507601NEWT:520NEWT:186441NEWT:634955NEWT:643680NEWT:214092NCBITaxon:6157NEWT:6239NEWT:13095NEWT:162425NEWT:104105NEWT:216257NEWT:102169NEWT:208893NEWT:9986NEWT:4054NEWT:8654NEWT:8658NEWT:1268063NEWT:8657NEWT:8655NEWT:5147NEWT:98351NEWT:1263854NEWT:118503NEWT:2059687NEWT:160488NEWT:63558NEWT:28104NEWT:207559NEWT:407821NCBITaxon:2NEWT:85057NEWT:985076NEWT:568708NEWT:1215323NEWT:986NEWT:52641NEWT:7159NEWT:267671NEWT:28532NEWT:7160NEWT:353152NEWT: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