{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD063207/2409_FK_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD063207/2409_FK_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD063207/2409_FK_11.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD063207/2409_FK_10.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD063207/2409_FK_7.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD063207/2409_FK_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD063207/2409_FK_12.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD063207/2409_FK_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD063207/2409_FK_8.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD063207/2409_FK_6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD063207/2409_FK_9.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD063207/2409_FK_4.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD063207/2409_FK_ALL.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["richard.wilson@utas.edu.au"],"submitter":["Richard Wilson"],"technology_type":["Mass Spectrometry","Data-independent acquisition","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Legume proteomics","Lc-ms profiling","Proteomics","Vicia faba","Fava bean proteomics"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD063207"],"tissue":["Seed"],"sample_protocol":["20 mg of each of the freeze-dried powdered samples were weighed into separate 2-ml SafeLock Eppendorf tubes. Three replicates of each tissue type were prepared . Phenolic compounds can interfere with protein extraction by forming insoluble complexes with proteins and other macromolecules, thereby reducing protein yield and purity. Their removal is essential to ensure accurate quantification and reliable downstream analyses such as spectrophotometry.  To remove interfering phenolic compounds, we used a method defined by Warsame et al., (2022). Briefly, cold (~4 ⸰C) aqueous acetone (80 % v/v) containing 5 mM sodium ascorbate was added to each sample at a 1:20 (w/v) sample-to-buffer ratio. The suspension was vortexed for 1 minute and centrifuged at 1500 × g for 10 minutes at 4 ⸰C. This step was repeated twice.  The sample was then washed with cold acetone  once, briefly air-dried then resuspended in either Tissue Protein Extraction Reagent (T-PER; Thermo Scientific) or 8 M urea, each containing protease inhibitors (cOmplete Mino protease inhibitor cocktail, EDTA-free; Merck). To compare methods, only reagents compatible with the BCA protein quantification assay were used, hence DTT and thiourea, which are common additives in chaotropic extraction buffers, were omitted. One millilitre of extraction buffer was added and the suspension was shaken at 300 rpm for 1 h at room temperature; samples were centrifuged at 1500 x g for 15 minutes at 4 ⸰C, and the supernatants were collected. Protein quantification was obtained by BCA assay using the Pierce BCA Assay Kit following standard assay procedures, after diluting the extract 1:2 in MilliQ  H2O. The standard curve was also prepared using the same dilution of buffer as a background.  A 30 µg protein aliquot of each sample was subjected to stepwise processing beginning with reduction using 10 mM dithiothreitol (DTT) at 4 ⸰C overnight . This was followed by alkylation with 50 mM iodoacetamide for 2 hours at room temperature. Proteolytic digestion was carried out using 1.2 µg of MS-grade trypsin/LysC (Promega, Madison, WI, USA), following the SP3  protocol (Hughes et al., 2019). After digestion, samples were acidified to 0.1 % with trifluoroacetic acid and centrifuged at 21,000 × g for 20 minutes to isolate peptides. The resulting peptide mixtures were desalted using ZipTips (Merck, Darmstadt, Germany) in accordance with the manufacturer’s instructions."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["The complete set of Vicia faba protein coding sequences were downloaded from NCBI (txid 3906; 38222 sequences downloaded on 13/06/2024) and Mercator4 (developer/reference?) was used to generate an annotated proteome by homology matching against verified protein sequences. The FASTA output file was then used to generate a spectral library of 22,645 proteotypic peptide sequences mapping to a total of 4,128 protein groups using the Pulsar search engine in Spectronaut. This library was then used for the targeted extraction of DIA-MS2 spectra and for relative quantification of proteins across the samples. Default (BGS Factory) settings were used for quantification and normalization, with the exception that proteins identified by a single peptide were excluded."],"omics_type":["Proteomics"],"labhead":["Dr Richard Wilson"],"instrument_platform":[""],"labhead_affiliation":["Proteomics facility, Central Science Laboratory, University of Tasmania"],"submission_type":["PARTIAL"],"species":["Vicia Faba"],"submitter_mail":["richard.wilson@utas.edu.au"],"publication":["10.1016/J.JFCA.2026.109121"],"submitter_affiliation":["University of Tasmania"],"submitter_country":["Australia"],"additional_accession":[]},"is_claimable":false,"name":"Proteomic profiling of fava bean tissues: Optimization of extraction method and comparative analysis using LC-MS","description":"Fava beans (Vicia faba) have demonstrated potential to replace traditional animal-based protein sources. The quantity and quality of protein found in fava beans makes them a potential candidate for sustainable protein alternative. However, the understanding of their proteomic profile remains limited. In this study, we present an optimized proteomic workflow for fava beans, comparing the extraction efficiency of detergent-based vs chaotrope-based extraction methods. We conducted liquid chromatography-mass spectrometry (LC-MS) using data-independent acquisition (DIA) to improve coverage and analysed the protein profiles of different fava bean tissues, including dried mature beans, freeze dried fresh whole beans, outer coat, and cotyledon (core). Our results reveal significant differences in protein composition between extraction methods and bean tissues, providing insights into the most effective approach for studying fava bean proteomes. Future studies can utilize this optimized workflow for the functional characterization of fava bean proteins, advancing the exploration of sustainable plant-based protein sources. This study provides a valuable resource for advancing proteomic research of legume species, contributing to more efficient proteomic profiling in plant 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