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Adoni"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Chymotrypsin","Missed cleavages","Sample preparation","Proteomics","Protein digestion"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD072165"],"tissue":["Leukocyte","Epithelial Cell","Cell Culture"],"sample_protocol":["Protein preparation For all experiments relating to the benchmarking of rChymoSelect against standard chymotrypsin (V1061, Promega), a standard human K562 intact extract (10mg/mL of human cell K562 lysed in 6 M Urea, Promega V6941) was used. For comparison of rChymoSe-lect to trypsin (Trypsin Gold, V5280, Promega); human bone osteosarcoma epithelial (U2-OS) cells were lysed in 100 mM Tris-Cl (pH8.5), 5% sodium dodecyl sulfate (SDS), 5mM Tris(2-carboxyethyl)phosphine hydrochlo-ride (TCEP) and 20mM chloroacetamide. Samples were boiled for 10 minutes and then cooled to room tempera-ture before being subjected to ultrasonic bath sonication for 10 minutes. Protein content was quantified via Bicin-choninic Acid (BCA) assay11 (ThermoFisher Scientific). Optimisation of in-solution and SP3 digestion 20µg of K562 lysate, was diluted to a final concentration of 2M, 4M and 6M urea for rChymoSelect, 2M and 0.6M urea for standard chymotrypsin and 0.6M urea for tryp-sin. All digestions were performed at 25°C for in-solution digestion, at 2- or 16-hours using a thermoshaker (Ep-pendorf) at 1500rpm. For SP3 digestion, the samples were prepared in a KingFisher APEX robot (ThermoFisher Sci-entific) using a protocol from Koenig et al12, with the fol-lowing modifications: the 96-well comb was stored in plate 1, plate 2 contained reconstituted sample in 70% acetonitrile with magnetic MagReSyn Hydroxyl beads in a protein/bead ratio of 1:2. Washing solutions were in plates 3–5 (95% acetonitrile) and plates 6–7 (70% etha-nol). Plate 8 contained 200 μL of digestion solution, which consisted of protease (rChymoSelect or standard chymotrypsin) in 50 mM ammonium bicarbonate (pH 8.5). For this optimisation, different protease/protein ratios (1:100, 1:40, 1:20) and guanindinium hydrochlo-ride (GND) concentrations (0.1M, 0.2M and 0.4M) were tested, with incubation for 2-hours, at 37°C. For both zdi-gestion protocols, protease activity was quenched by acidification with trifluoroacetic acid (TFA) to pH 2 be-fore the resulting peptide-mixture was desalted on an OASIS HLB 96-well plate (Waters), before drying in-vacuo using a Savant DNA120 (ThermoFisher Scientific). Comparison of Trypsin and rChymoSelect with deep offline fractionation 200 µg of proteins from U2-OS cells lysed in SDS buffer were prepared using the SP3 lysis method and digested with either trypsin overnight or rChymoSelect for 2h at 37 °C. Digestion was quenched by TFA, and peptides were desalted using the OASIS HLB 96-well plate (Waters). Pep-tides were then fractionated with a Vanquish HPLC (Thermo Fisher Scientific) using an Acquity BEH C18 col-umn (2.1 x 50 mm with 1.7µm particles, Waters), mobile phase A: 10 mM ammonium formate, pH 10, mobile phase B: 80% acetonitrile, 10mM ammonium formate, pH10, with a flow rate of 1000µL/min. 24 fractions were col-lected across a 6-minute gradient. Fractions were then dried and reconstituted in 0.5% TFA before undergoing liquid chromatography–tandem mass spectrometry (LC-MS/MS) analysis. LC-MS/MS  Peptides were reconstituted in 0.5% TFA, and 500ng were injected on an UltiMate 3000 RSLCnano liquid chromatog-raphy system (Thermo Fisher Scientific). A 5.5 cm μPAC Neo HPLC analytical column (COL-CAPHTNEOB) was connected to a Silica Tip emitter. Column temperature was set at 45°C, and column flow rate was set to 1500 nL/min. Mobile phase A (0.1% formic acid) and mobile phase B (80% acetonitrile, 0.1% formic acid) were ap-plied with an elution gradient from 1.0 to 35.0% mobile phase B over either 25 minutes (for the fractionations) or 51 minutes (protocol optimization). Peptides were ion-ized using a spray voltage of 2.0 kV (275°C). The mass spectrometer was set to acquire full-scan MS spectra (350 to 1400 m/z) for a maximum injection time set to Auto at a resolution of 120,000 and an automated gain control (AGC) target value of 250%. The instrument was set up in DDA with a Wide Window Acquisition (4th window) for all the precursors with a charge state in range of 2+ to 5+; most abundant ions were then fragmented in HCD (30% normalized collision energy) with MS2 acquisition at a resolution of 30,000, AGC: 400%, maximum injection time: Dynamic, dynamic exclusion: 20s. For protocol op-timization with Data-Independent Acquisition: 56 win-dows of 12 Da (m/z range 361-1033) were fragmented via HCD with normalized energy: 30%, AGC: 1000% and reso-lution: 15,000."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Data Analysis  MS data were searched against the Human SWISS-Prot protein database (August 2023) with SAGE proteomics software for downstream analysis13 (for DDA). The in-creased capacity to handle large search space (due to in-creased cleavage sites and missed cleavages), as well as its fast performance made it an appropriate software choice for this work14. For cleavage specificity analysis, the following parameters were set: cleavage sites: F, Y, W, L, K, R, H, N, Q (except before P), missed cleavages: 6. For onward analysis, cleavage sites: FYWL (except before P), missed cleavages 3. For all searches, variable modifica-tions: [+15.9949, M]; static modifications: [+57.0215, C], max variable modifications: 3. PSMs with q-value<0.01 were selected for onward analysis, ambiguous proteins and contaminants were filtered out. Further, all validated proteins were identified in at least 2 of 3 biological repli-cates. Raw SAGE search outputs were processed with the PickedGroupFDR pipeline15 to produce a com-bined_protein.tsv file that was used for protein quantifica-tion and downstream enrichment analyses. Peptide-protein rollup and proteingroup collapsing were per-formed using the PickedGroupFDR implementation. Downstream statistics, plotting and figure generation were performed in GraphPad Prism16.  For Data-Independent Analysis (DIA), RAW data was processed with FragPipe v23.117, with enzyme: chymotrypsin cleav-age sites: F, L, W, Y, (except before P), missed cleavages: 1, variable modifications: [+15.9949, M], [+42.0106, Nt], fixed modifications: [C, +57.02146] and modifications per peptide: 3. For DIA library-based searches, the DDA RAW files from the corresponding runs were used to generate a spectral library, using DIA-NN18"],"omics_type":["Proteomics"],"labhead":["Konstantinos Thalassinos"],"instrument_platform":[""],"labhead_affiliation":["UCL"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["kish.95@live.com"],"publication":["41961476 Adoni KR, Ditcham JE, González Rivera AK, Charlton GH, Saveliev SV, Thalassinos K, Zenezini Chiozzi R. Enhanced Proteomics Analysis with a Novel Recombinant Chymotrypsin Analogue Engineered for High Cleavage Specificity. J Proteome Res. 2026 25(5):2511-2519 10.1021/acs.jproteome.5c01262"],"submitter_affiliation":["University College London"],"submitter_country":["United Kingdom"],"pubmed_abstract":["Chymotrypsin is widely used in shotgun proteomics, owing to its orthogonal cleavage specificity relative to trypsin, which enhances sequence coverage of hydrophobic protein regions. However, commercial preparations often display variable cleavage specificity, trypsin contamination, and elevated missed cleavage rates, which can collectively reduce the proteome coverage and data reproducibility. To address these limitations, we present a novel recombinant chymotrypsin (<i>rChymoSelect</i>) engineered for improved cleavage specificity and robustness in proteomics workflows. Benchmarking against standard bovine chymotrypsin revealed 97% C-terminal cleavages after tyrosine (Y), phenylalanine (F), and leucine (L) for <i>rChymoSelect</i>, compared to 72% for the standard enzyme. This enhanced cleavage specificity reduced missed cleavages and increased peptide-spectrum matches across charge states. Across 3,638 identified proteins, <i>rChymoSelect</i> yielded 22.2% unique identifications compared with 8.2% for standard chymotrypsin, while maintaining similar peptide length, <i>m</i>/<i>z</i>, and hydrophobicity distributions. The enzyme remained active in up to 6 M urea and achieved near-maximal proteome coverage within 2 h (only a 2.4% gain after overnight digestion). These results establish <i>rChymoSelect</i> as an advanced tool with improved cleavage specificity that reduces analytical complexity and enhances the reliability of proteomic analysis, while expanding chymotryptic digestion to hydrophobic and high-denaturant proteomics applications."],"pubmed_title":["Enhanced Proteomics Analysis with a Novel Recombinant Chymotrypsin Analogue Engineered for High Cleavage Specificity."],"pubmed_authors":["Adoni Kish R KR, Ditcham Jonathan E JE, González Rivera Alba Katiria AK, Charlton Georgina H GH, Saveliev Sergei V SV, Thalassinos Konstantinos K, Zenezini Chiozzi Riccardo R"],"additional_accession":[]},"is_claimable":false,"name":"Enhanced Proteomics Analysis with a Novel Recombinant Chymotrypsin Analogue En-gineered for High Cleavage Specificity","description":"Chymotrypsin is widely used in shotgun proteomics owing to its orthogonal cleavage specificity relative to trypsin, which enhances sequence coverage of hydrophobic protein regions. However, commercial preparations often display variable cleavage specificity, trypsin contamination, and elevated missed-cleavage rates, which collectively can reduce proteome coverage and data reproducibility. To address these limitations, we present a novel recombinant chymotrypsin (rChymoSelect) engineered for improved cleavage specificity and robustness in proteomics workflows. Benchmarking against standard bovine chymotrypsin revealed 97 % C-terminal cleavages after tyrosine (Y), phenylalanine (F), and leucine (L) for rChymoSelect, compared with 72 % for the standard enzyme. This enhanced cleavage specificity re-duced missed cleavages and increased peptide-spectrum matches across charge states. Across 3,638 identified proteins, rChymoSelect yielded 22.2 % unique identifications compared with 8.2 % for stand-ard chymotrypsin, while maintaining similar peptide length, m/z, and hydrophobicity distributions. No-tably, rChymoSelect showed enriched recovery of mitochondrial proteins, consistent with its improved digestion of hydrophobic targets. The enzyme remained active in up to 6 M urea and achieved near-maximal proteome coverage within 2 hours (only a 2.4 % gain after overnight digestion). Integration with data-independent acquisition (DIA) increased total protein identifications from approximately 2,200 (DDA) to 3,200 (DIA), a 45 % gain, with rChymoSelect outperforming standard chymotrypsin by 16.6–22.4 % in peptide-spectrum matches and 4.6–6.2 % in protein identifications. These results estab-lish rChymoSelect as an advanced tool with improved cleavage specificity that reduces analytical com-plexity, and enhances the reliability of proteomic analysis, while expanding chymotryptic digestion to hydrophobic and high-denaturant proteomics applications.","dates":{"publication":"2026-06-08","submission":"2025-12-18"},"accession":"PXD072165","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:2042546","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:661410","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:3767","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:44250","NEWT:317447","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:12637","NEWT:2164133","NEWT:2767846","NEWT:314344","NEWT:108061","NEWT:224308","NEWT:49928","NEWT:160621","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1310173","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:550537","NEWT:284812","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:215451","NEWT:460519","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2499525","NEWT:142786","NEWT:2853422","NEWT:487","NEWT:1679718","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:987059","NEWT:491","NEWT:460523","NEWT:85694","NEWT:85692","NEWT:3750","NEWT:291146","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:445","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:219798","NEWT:548","NEWT:150475","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:8673","NEWT:550","NEWT:10804","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","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:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:52641","NEWT:353152","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:13037","NEWT:519","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","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:510516","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:287889","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:315750","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:1436183","NEWT:4232","NEWT:9922","NEWT:416348","NEWT:11298","NEWT:4236","NEWT:398031","NEWT:196627","NEWT:523840","NEWT:1076878","NEWT:200308","NEWT:200302","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:2666255","NEWT:999810","NEWT:28995","NEWT:1392998","NEWT:1150621","NEWT:1085791","NEWT:745531","NEWT:226900","NEWT:231490","NEWT:590651","NEWT:449239","NEWT:244704","NEWT:9909","NEWT:9902","NEWT:430615","NEWT:563041","NEWT:36599","NEWT:41949","NEWT:326423","NEWT:326424","NEWT:13013","NEWT:749906","NEWT:418985","NEWT:749907","NEWT:431947","NEWT:142809","NEWT:1095183","NEWT:302409","NEWT:9979","NEWT:130821","NEWT:2320211","NEWT:27606","NEWT:290610","NEWT:1519788","NEWT:59202","NEWT:9975","NEWT:8643","NEWT:1801631","NEWT:1159899","NEWT:502780","NEWT:860688","NEWT:35231","NEWT:1774208","NEWT:8644","NEWT:1125630","NEWT:28930","NEWT:202914","NEWT:222523","NEWT:27602","NEWT:502779","NEWT:297246","NEWT:483139","NEW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