{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD072578/Tears_peptidome_unmod_1_pyroGlu_250903_VC_tear_peptide_1.raw.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD072578/Tears_peptidome_unmod_pooled_VC_pyroGlu_250909_VC_tear_peptide_pooled_1.raw.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD072578/Lacritin_PRP_endogenous_glycopeps_250903_VC_tear_peptide_1.raw.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD072578/Tears_peptidome_unmod_3_pyroGlu_250903_VC_tear_peptide_3.raw.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD072578/Lacritin_PRP_endogenous_glycopeps_250903_VC_tear_peptide_2.raw.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD072578/Lacritin_PRP_endogenous_glycopeps_250909_VC_tear_peptide_pooled_1.raw.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD072578/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD072578/250903_VC_tear_peptide_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD072578/250903_VC_tear_peptide_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD072578/250909_VC_tear_peptide_pooled_1.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["stacy.malaker@yale.edu"],"submitter":["Vincent Chang"],"technology_type":["Data-dependent acquisition","Glycoproteomics","Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Tear fluid","Glycoproteomics","Proteolysis","Glycopeptidome","Cleavage","Mass spectrometry","Peptidome"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD072578"],"tissue":["Tear"],"sample_protocol":["Tear fluid Sample collection Tear fluid was purchased from Innovative Research (obtained via microcapillary collection) and stored at −20°C until further processing. 2 individual donors and 1 pooled sample (56669-ND0557-CF35, 56668-ND0350-CF42, and 56667-ND0143-CF43) was used for downstream MS analysis.  Mass spectrometry sample preparation with FASP Freshly thawed tear fluid proteins from each patient were diluted to a final concentration of 0.2 mg/mL in 100 µL of 20 mM Tris. DTT was then added to a concentration of 2 mM and reacted at 65 °C for 1 hour followed by alkylation in 5 mM IAA for 15 min in the dark at RT. Subsequently, samples were loaded onto a 10kDa filter and the filtrate was collected over two elutions (200 µL of 20mM Tris for each elution). The filtrate was acidified by adding 4 µL of formic acid and desalted before injection into the mass spectrometer. Desalting was performed using 10 mg Strata-X 33 µm polymeric reversed phase SPE columns (Phenomenex). Each column was activated using 500 µL of acetonitrile (ACN) (Honeywell) followed by of 500 µL of 0.1% formic acid, 500 µL of 0.1% formic acid in 40% ACN, and equilibration with two additions of 500 µL of 0.1% formic acid. After equilibration, the samples were added to the column and rinsed twice with 200 µL of 0.1% formic acid. The columns were transferred to a 1.5 mL tube for elution by two additions of 150 µL of 0.1% formic acid in 40% ACN. The eluent was then dried using a vacuum concentrator (LabConco) prior to reconstitution in 10 µL of 0.1% formic acid. The resultant peptides were then injected onto a Dionex Ultimate3000 coupled to a Thermo Orbitrap Eclipse Tribrid mass spectrometer. We employed a higher-energy collision dissociation product-dependent electron transfer dissociation (HCD-pd-ETD) method; in some cases, we used supplemental activation in ETD (EThcD). The files were searched using Byonic, followed by manual data curation."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Mass spectrometry data analysis Raw files were searched using Byonic (version 4.5.2, Protein Metrics, Inc.) against the UniProtKB/Swiss-Prot Homo sapiens proteome (Query: proteome:up000005640 AND reviewed:true) For all samples, we used the default O-glycan database containing 9 common structures. First, raw files were searched against the human proteome (without glycan modifications) to generate a focused protein database. This focused database was then used for an additional search with an O-glycan database. Files were searched with nonspecific cleavage and an unrestricted amount of missed cleavages. Samples treated with trypsin were searched with the same parameters but also allowed cleavage C-terminal to Arg or Lys. Mass tolerance was set to 10 ppm for MS1’s and 20 ppm for MS2’s. Pyroglutamylation and deamidation was set as a variable modification and carbamidomethyl Cys was set as a fixed modification. From the Byonic search results, glycopeptides were filtered to a score of >200 and a logprob of >2. From the remaining list of glycopeptides, the extracted ion chromatograms, full mass spectra (MS1s), and fragmentation spectra (MS2s) were investigated in XCalibur QualBrowser (Thermo) to generate a list of true-positive glycopeptides, as reported in Table 2. Each reported glycopeptide listed in Table 2 was manually validated from the filtered list of Byonic’s reported peptides (score>200 and logprob >2) according to the following steps: The MS1 was first used to confirm the precursor mass and chosen isotope was correct. This also allowed us to identify any co-isolated species that could interfere with the MS2s and/or explain unassigned peaks. The HCD and EThcD fragmentation spectra were then investigated to identify sufficient coverage to make a sequence assignment. When possible, multiple MS2 scans were averaged to obtain a stronger spectrum. For HCD, an initial glycopeptide identification was confirmed if the presence of the precursor mass without a glycan present (i.e., Y0), along with coverage of b and y ions without glycosylation. For longer peptides, we required the presence of Y0 and fragments that were expected to be abundant (e.g., N-terminally to Pro, C-terminally to Asp). When the peptide contained a Pro at the C-terminus, the bn-1 was considered sufficient. Further, when the sequence contained oxidized Met, the Met loss from the bare mass was considered as representative of the naked peptide mass. We then used electron-based fragmentation MS2 spectra for localization. Here, all plausible localizations were considered, regardless of search result output. We confirmed the presence of fragment ions in ETD or EThcD that were between potential glycosylation sites, if sufficient c/z ions were present then a glycan mass was considered localized. For glycopeptide manual validation, extracted ion chromatograms are evaluated at the MS1 level to determine the charge and m/z of the highest abundance precursor species. Mass spectrometry data files and raw search output can be found on PRIDE with identifier _____"],"omics_type":["Proteomics"],"labhead":["Stacy Malaker"],"instrument_platform":[""],"labhead_affiliation":["Department of Chemistry"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["10.1021/JACSAU.6C00834"],"submitter_mail":["vincent.chang@yale.edu"],"submitter_affiliation":["Yale University"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"O-glycosylation affects proteolysis of the native tear peptidome","description":"The endogenous tear peptidome plays essential roles in maintaining ocular homeostasis by stimulating immune response and participating in antimicrobial activity. The biological function of these native peptides is governed by their biochemical properties including peptide length, charge, and hydrophobicity. Accordingly, the production of native peptides within the tear film is tightly regulated through a complex interplay between circulating proteases and the proteolytic susceptibility of the protein substrate. Though glycosylation has been shown to regulate the proteolysis of specific proteins in vitro, the extent to which endogenous cleavage motifs are mediated by proximal O-glycans remains unexplored in a more complex sample. Furthermore, the existence and identity of native tear peptides bearing O-glycans has yet to be elucidated, largely due to the high analytical complexity of tear fluid and the difficulty in characterizing O-glycosylated peptides. To address this gap, we leveraged advances in mass spectrometry (MS) to provide the first observation of circulating tear O-glycopeptides, detailing their biochemical properties and overall glycan compositions. Beyond systematic profiling of the O-glycopeptidome, we employed site-specific glycoproteomic analysis followed by molecular dynamics to investigate the interplay between O-glycan proximity and proteolysis. Here, we observed that O-glycans preferentially occupy glycosites distal from the N-/C-terminus, thereby influencing distinct cleavage motifs and peptide backbones. Finally, we showed in silico that O-glycosylation can mediate the solvent accessibility of proximal cleavage residues, thus providing a structural basis for these observations. Taken together, this study defines the proteolytic landscape at the ocular surface and highlights a potential role for tear fluid 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