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Levin"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Lc-ms","Proteomics","Chromophores","Nhs chemistry","Uvpd"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD075227"],"tissue":["Kidney"],"sample_protocol":["Expi 293F cell pellet was solubilised in lysis buffer (1% SDS, 50 mM TEAB) and either treated with Benzonase or sonicated in Bioruptor Pico. Extracted proteins were then reduced (TCEP) and alkylated (2-CAA). Free amines were dimethyl labelled with formaldehyde and cyanoborohydride. The reaction was quenched, labelled peptides were precipitated by adding methanol, chloroform and water. The protein pellet was washed with methanol, resuspended in 1% SDS in 50 mM TEAB buffer and digested using a modified SP3 protocol. Peptides were labelled with approximately 100 nmol of each aromatic label (in neat acetonitrile or DMSO) per µg of peptide for two hours at room temperature. Labelled peptides weredesalted using Oasis HLB 96-well plates. LC-MS/MS data were acquired using an UltiMate 3000 nanoUHPLC system coupled to an Orbitrap Exploris 480 (both Thermo Fisher Scientific) modified with an Omnitrap (Fasmatech). The Omnitrap is equipped with a 193 nm ArF excimer laser (Coherent) with a repetition rate of 200 Hz and a maximum pulse energy of 12 mJ. Peptides were trapped on a C18 PepMap100 pre-column using solvent A (0.1% formic acid in water), then separated on an in-house packed analytical column (50 µm i.d. x 50 cm in-house packed). The composition of solvent B (0.1% formic acid in acetonitrile) changed from 12% to 40% over 15 min. Full scan MS1 spectra were acquired in the Orbitrap (scan range 350-1400 m/z, resolution 60000, AGC target 300%). Top 10 most abundant peptides were selected each round of DDA for fragmentation. UVPD was performed in the Omnitrap; its products were mass-analysed in the Orbitrap at 30000 resolving power, the AGC value was set to 200%, and the maximum injection time was set to 50 ms."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Raw data were analyzed using FragPipe (v23.1) MSFragger 4.3 with standard ‘closed’ search settings against Uniprot database (UPR_Homo sapiens_9606 accessed on 24.10.29). The number of missed cleavages was set to two when searching trypsin data (allowed cuts only after arginine residues) and to four when searching ArgC data. Lysine dimethylation and cysteine carbamidomethylation were set as fixed modifications. Methionine oxidation and N-terminal derivatization were set as variable modifications. Mass accuracy was specified to 20 ppm for fragment ions and 10 ppm for precursor ions. Data were searched using b and y ion series. MSBooster and all quantification parameters were disabled. Results were reported at 1% protein-level FDR. Lists of peptide-spectrum matches (PSMs) (“psm.tsv”) generated by MSFragger were processed using in-house developed R scripts (RStudio, build 387)."],"omics_type":["Proteomics"],"labhead":["Shabaz Mohammed"],"instrument_platform":[""],"labhead_affiliation":["The Rosalind Franklin Institute; University of Oxford, Department of Biochemistry; University of Oxford, Department of Chemistry"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["41881472 Levin N, Demyanenko Y, Kitano E, Mohammed S. Investigating the Efficiency of Ultraviolet Photodissociation in Peptides Modified with &lt;i&gt;N&lt;/i&gt;-Terminal UV-Absorbing Chromophores. J Am Soc Mass Spectrom. 2026 37(5):1124-1131 10.1021/jasms.5c00389"],"submitter_mail":["nikita.levin@rfi.ac.uk"],"submitter_affiliation":["University of Oxford"],"submitter_country":["United Kingdom"],"pubmed_abstract":["Ultraviolet photodissociation (UVPD) has emerged as a powerful alternative to conventional collision-induced dissociation (CID) for peptide and protein sequencing in mass spectrometry-based proteomics. However, the UVPD efficiency depends on the presence of UV-absorbing chromophores within analytes. Here, we systematically investigate how <i>N</i>-terminal modification of peptides with aromatic chromophores influences the 193 nm UVPD efficiency and fragmentation behavior. Using NHS ester chemistry, human cell lysate digests were derivatized with a range of UV-absorbing aromatic labels and analyzed on an Omnitrap-Orbitrap platform equipped with a 193 nm ArF excimer laser. Compared with unmodified controls, derivatized peptides displayed a modestly increased fragmentation efficiency and a greater diversity of sequence-informative fragments, particularly <i>b</i>-type ions. Peptides lacking aromatic amino acids benefited most from N-terminal aromatic labeling, exhibiting enhanced fragmentation and sequence coverage. These findings demonstrate that incorporation of aromatic chromophores at the N-terminus can enhance UVPD performance and improve spectral interpretability, thereby expanding the applicability of UVPD in bottom-up proteomics workflows."],"pubmed_title":["Investigating the Efficiency of Ultraviolet Photodissociation in Peptides Modified with &lt;i&gt;N&lt;/i&gt;-Terminal UV-Absorbing Chromophores."],"pubmed_authors":["Levin Nikita N, Demyanenko Yana Y, Kitano Eduardo E, Mohammed Shabaz S"],"additional_accession":[]},"is_claimable":false,"name":"UVPD of peptides modified with N-terminal UV-absorbing chromophores","description":"Ultraviolet photodissociation (UVPD) has emerged as a powerful alternative to conventional collision-induced dissociation (CID) for peptide and protein sequencing in mass spectrometry–based proteomics. However, UVPD efficiency depends on the presence of UV-absorbing chromophores within analytes.The uploaded dataset is a systematic investigation of how N-terminal modification of peptides with aromatic chromophores influences 193 nm UVPD efficiency and fragmentation behavior. Using NHS ester chemistry, human cell lysate digests were derivatized with a range of UV-absorbing aromatic labels and analyzed on an Omnitrap–Orbitrap platform equipped with a 193 nm ArF excimer laser. Compared with unmodified controls, derivatized peptides displayed modestly increased fragmentation efficiency and greater diversity of sequence-informative fragments, particularly b-type ions. Peptides lacking aromatic amino acids benefited most from N-terminal aromatic labeling, exhibiting enhanced fragmentation and sequence coverage. These findings demonstrate that incorporation of aromatic chromophores at the N-terminus can enhance UVPD performance and improve spectral interpretability, thereby expanding the applicability of UVPD in bottom-up proteomics 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