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Wang"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Apis mellifera venom","Proteomics","Trpv1","Inflammation","Peptidomics","Pull-down","Macrophage"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD075103"],"tissue":["Venom","Macrophage"],"sample_protocol":["Crude Apis mellifera venom was fractionated by AKTA chromatography. Individual fractions were analyzed by SDS–PAGE, and visible protein bands were excised, destained, reduced, alkylated, and subjected to in-gel enzymatic digestion prior to LC–MS/MS analysis for protein identification. Protein identification was performed using an Orbitrap Fusion mass spectrometer coupled to an EASY-nLC 1000 system (Thermo Fisher Scientific). Peptides were separated on a C18 column (Acclaim PepMap, 100 μm id × 2 cm, 3 μm particle size) using a 60 min linear gradient at 300 nL/min with 0.1% formic acid in water (mobile phase A) and 0.1% formic acid in acetonitrile (mobile phase B). Fraction F4 was subjected to 3 kDa ultrafiltration (Millipore) to enrich low-molecular-weight peptides (<3 kDa), followed by C18 solid-phase extraction for desalting and concentration. The resulting peptide samples were analyzed by nano LC–MS/MS under the same instrumental conditions for peptidomics characterization. For GST pull-down experiments, purified GST-TRPV1 or GST control proteins were immobilized on glutathione resin, incubated with fraction F4 peptide samples (after concentration and salt removal), washed, and eluted. The eluted samples were further purified, filtered, concentrated, and analyzed by nano LC–MS/MS under the same instrumental conditions. Macrophage proteomic profiling was performed using an Orbitrap Exploris 480 mass spectrometer coupled with an EASY-nanoLC 1200 system (Thermo Fisher Scientific). Peptides were separated on a 75 μm × 20 cm C18 analytical column using a 60 min gradient at 300 nL/min. Raw data were acquired using Thermo Xcalibur software."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["For gel-based protein identification, raw MS and MS/MS spectra were processed using Proteome Discoverer (v2.4, Thermo Fisher Scientific) and searched against the Apis FASTA database downloaded from UniProtKB (taxonomy ID: 7459; 98,839 entries; accessed on October 10, 2023). For peptidomic analyses, raw MS/MS files were processed using PEAKS X Pro (PEAKS Studio 10.6; Bioinformatics Solutions Inc., Waterloo, Canada) using a de novo sequencing workflow. The precursor mass tolerance was set to 20 ppm and fragment ion tolerance to 0.02 Da. No enzyme specificity was applied. Variable modifications included oxidation, deamidation, and protein N-terminal acetylation, allowing up to three variable post-translational modifications per peptide. Peptide sequences with ALC ≥ 50% were deposited and used to construct an in-house Apis mellifera venom peptide database. Peptides with ALC ≥ 80% and non-zero peak area were considered high-confidence endogenous peptides. For GST pull-down experiments, candidate TRPV1-associated peptides were identified using PEAKS de novo sequencing and the PEAKS DB algorithm against the in-house Apis mellifera venom peptide database described above. For macrophage proteomic analysis, protein identification and label-free quantification (LFQ) were performed using MaxQuant (version 2.6.5.0). The reference protein database was retrieved from the reviewed UniProt Mouse proteome (taxonomy ID: 10088; 17,285 entries; accessed on September 4, 2024). Trypsin was specified as the digestion enzyme, allowing up to two missed cleavages. Carbamidomethylation of cysteine was set as a fixed modification, and oxidation of methionine and protein N-terminal acetylation were set as variable modifications. A false discovery rate (FDR) of 1% was applied at both peptide and protein levels. The MaxQuant output file (MacrophageProteomics_proteinGroups.txt) contains all experimental conditions analyzed in the MaxQuant project. For analyses reported in the associated manuscript, dexamethasone- and peptide P4–treated samples were not included. Corresponding columns were excluded, and proteins detected exclusively in those samples were removed. The manuscript-specific dataset is provided as MacrophageProteomics_proteinGroups_filtered_NoDXMSNoP4.xlsx."],"omics_type":["Proteomics"],"labhead":["Hongcheng Zhang"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["State Key Laboratory of Resource Insects, Institute of Apicultural Research, Chinese Academy of Agricultural Sciences"],"species":["Apis Mellifera (honeybee)","Mus Musculus (mouse)"],"publication":["10.1021/ACS.JNATPROD.5C01554"],"submitter_mail":["1029020173@qq.com"],"submitter_affiliation":["University of Liège; Institute of Apicultural Research, Chinese Academy of Agricultural Sciences"],"submitter_country":["China"],"additional_accession":[]},"is_claimable":false,"name":"Peptidomics-guided identification of TRPV1-targeting peptides from Apis mellifera venom and macrophage proteomics","description":"Bee venom has been traditionally used in the treatment of inflammatory disorders and is known to contain diverse bioactive peptide components. In this study, we systematically characterized the Apis mellifera venom peptidome and investigated peptides enriched under TRPV1 pull-down conditions with potential inflammatory modulatory activity. Crude venom was fractionated by AKTA chromatography, and individual fractions were evaluated by SDS–PAGE. Protein bands were subjected to in-gel digestion followed by LC–MS/MS protein identification. Fraction F4, which displayed a prominent A280 absorbance peak during AKTA chromatography, was further analyzed by LC–MS/MS–based peptidomics. De novo sequencing results from fraction F4 were used to construct an in-house custom peptide database. Two independent GST pull-down workflows (exploratory and in-house) were performed using GST-TRPV1 and GST controls. Candidate peptides enriched in the GST-TRPV1 pull-down relative to GST controls were identified following background subtraction and peak-area filtering criteria. Selected synthetic peptide candidates were subsequently evaluated using macrophage-based proteomics experiments to assess their potential inflammatory modulatory effects. The deposited dataset includes raw LC–MS/MS files and processed outputs for gel-based protein identification, venom peptidomics, pull-down–associated peptide identification, macrophage proteomics (MaxQuant analysis), and the custom venom peptide FASTA library used for database searches.","dates":{"publication":"2026-04-17","submission":"2026-03-02"},"accession":"PXD075103","cross_references":{"TAXONOMY":["NEWT:3555","NEWT:71647","NEWT:330879","NEWT:260201","NEWT:35554","NCBITaxon:12939","NEWT:32046","NEWT:544496","NEWT:59529","NEWT:2042546","NEWT:32049","NEWT:1392696","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:45351","NEWT:445974","NEWT:43179","NEWT:180454","NEWT:5722","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:10245","NEWT:55153","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:351581","NEWT:43186","NEWT:428146","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:498019","NEWT:1351","NEWT:1438992","NEWT:1352","NEWT:2649997","NEWT:1147161","NEWT:661410","NEWT:638632","NEWT:263737","NEWT:224326","NEWT:1333499","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:5702","NEWT:95648","NEWT:1589","NEWT:135622","NEWT:1349","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:383379","NEWT:1401257","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:44491","NEWT:641809","NEWT:27933","NEWT:556484","NEWT:317447","NEWT:4688","NEWT:7955","NEWT:7719","NEWT:7959","NEWT:2261","NEWT:868565","NEWT:94323","NEWT:31156","NEWT:3112","NEWT:79329","NEWT:4442","NEWT:192875","NEWT:1214915","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:284218","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:1316931","NEWT:224308","NEWT:3347","NEWT:511145","NEWT:160621","NEWT:212790","NEWT:931281","NEWT:4432","NEWT:5762","NEWT:5763","NEWT:658457","NEWT:1310161","NEWT:77133","NEWT:295358","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:2246","NEWT:2652724","NEWT:5757","NEWT:68415","NCBITaxon:4563","NEWT:5755","NEWT:44688","NEWT:44689","NEWT:44447","NEWT:752555","NEWT:498211","NEWT:5759","NEWT:347256","NEWT:1736231","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:1392","NEWT:498217","NEWT:498216","NEWT:2242","NEWT:11320","NEWT:286","NEWT:391619","NEWT:246196","NEWT:287","NEWT:246197","NEWT:145458","NEWT:633149","NEWT:1149786","NEWT:10239","NEWT:68895","NEWT:44685","NEWT:161934","NEWT:4897","NEWT:1148","NEWT:5744","NEWT:72901","NEWT:213863","NEWT:5508","NEWT:3329","NEWT:5507","NEWT:410661","NEWT:55571","NEWT:35500","NEWT:1235816","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:4896","NEWT:1287689","NEWT:1390","NEWT:11557","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:294","NEWT:1773","NEWT:1182590","NEWT:3712","NEWT:82380","NEWT:3711","NEWT:935293","NEWT:375146","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:1772","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:263","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:11988","NEWT:284812","NEWT:8175","NEWT:400667","NEWT:43330","NEWT:1603293","NEWT:408169","NEWT:44664","NEWT:47946","NEWT:459758","NEWT:3702","NEWT:1245466","NEWT:243277","NEWT:1246791","NEWT:7067","NEWT:118694","NEWT:586722","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:274","NEWT:7070","NCBITaxon:287","NEWT:408172","NEWT:408170","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:1436733","NEWT:460519","NEWT:1247411","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1303443","NEWT:9483","NEWT:333760","NEWT:34607","NEWT:56636","NEWT:1513458","NEWT:1233681","NCBITaxon:40559","NEWT:506599","NEWT:2853422","NEWT:81077","NEWT:84588","NEWT:1679718","NEWT:480","NEWT:65349","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:300852","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:508771","NEWT:1883446","NEWT:253","NCBITaxon:2759","NEWT:1233435","NEWT:93061","NEWT:93062","NEWT:34613","NCBITaxon:4932","NEWT:109760","NEWT:29031","NEWT:943274","NEWT:644223","NEWT:235443","NEWT:108458","NEWT:5936","NEWT:272623","NEWT:272624","NEWT:320637","NEWT:886559","NEWT:3750","NEWT:55521","NEWT:983964","NEWT:118499","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:1130798","NEWT:55529","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:476272","NEWT:3747","NEWT:195051","NEWT:3988","NEWT:1116234","NEWT:561007","NEWT:1255228","NEWT:649908","NEWT:410289","NEWT:373153","NEWT:3983","NEWT:203696","NEWT:472","NEWT:352472","NEWT:97441","NEWT:1071661","NEWT:1202531","NEWT:1202532","NEWT:360094","NEWT:1408223","NEWT:470","NEWT:1408224","NEWT:41364","NEWT:5911","NEWT:1313","NEWT:1218097","NEWT:1080348","NCBITaxon:50557","NEWT:1314","NEWT:39251","NEWT:39491","NEWT:212142","NCBITaxon:5811","NEWT:29491","NEWT:101841","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:571256","NEWT:40483","NEWT:63366","NEWT:63367","NEWT:688333","NEWT:215402","NCBITaxon:548681","NEWT:318586","NCBITaxon:5820","NEWT:1547","NEWT:272634","NEWT:198107","NEWT:9031","NEWT:27292","NEWT:1872122","NEWT:1308","NEWT:7091","NEWT:1034015","NEWT:760568","NEWT:141262","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:4087","NEWT:9778","NEWT:306","NEWT:150475","NEWT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