{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074176/checksum.txt"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074176/22-Prot-0167_RC6_1_8184.d.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074176/22-Prot-0163_RC2_1_8193.d.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074176/22-Prot-0168_RC7_1_8201.d.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074176/22-Prot-0164_RC3_1_8195.d.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074176/22-Prot-0161_RB8_1_8175.d.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074176/MQ_Peak.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074176/22-Prot-0165_RC4_1_8196.d.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074176/22-Prot-0166_RC5_1_8183.d.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074176/22-Prot-0163_RC2_1_8178.d.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074176/22-Prot-0165_RC4_1_8181.d.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074176/22-Prot-0169_RC8_1_8202.d.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074176/22-Prot-0166_RC5_1_8198.d.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074176/22-Prot-0162_RC1_1_8177.d.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074176/22-Prot-0162_RC1_1_8192.d.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074176/MQ_Search.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074176/22-Prot-0169_RC8_1_8187.d.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074176/22-Prot-0160_RB7_1_8174.d.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074176/22-Prot-0164_RC3_1_8180.d.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074176/22-Prot-0161_RB8_1_8190.d.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074176/22-Prot-0167_RC6_1_8199.d.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074176/22-Prot-0168_RC7_1_8186.d.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074176/22-Prot-0160_RB7_1_8189.d.rar"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["christopher.gerner@univie.ac.at"],"submitter":["Christopher Gerner"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Mesoporous silica nanoparticles (msn); peptide delivery; peptide drugs; proteomics","proteomics","peptide drugs","peptide delivery","Mesoporous silica nanoparticles (msn)","Insulin"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD074176"],"tissue":["Colonic Epithelium Cell Line"],"sample_protocol":["To perform proteomic analysis, 600,000 cells were seeded in T75 flasks using 10 mL of complete cell culture medium. The cells were incubated for 48 h at 37ºC, and once confluent, treatments with insulin-loaded MSN (MSN(Ins), PEG-MSN(Ins), or PO3-MSN(Ins)) were applied at an equivalent insulin concentration of 10 µg mL-1, as in non-confined insulin as control (Ins(+)). All treatments were prepared in an insulin-free cell culture medium. A negative control (starved cells without insulin, Ins(‒)) was additionally tested via incubation with an insulin-free cell culture medium. After 6 h incubation at 37ºC, the cells were lysed under mechanical shear stress using isotonic lysis buffer (10 mM HEPES/NaOH, pH 7.4, 0.25 M sucrose, 10 mM NaCl, 3 mM MgCl2, 0.5% Triton X-100), supplemented with Protease and Phosphatase Inhibitor Cocktail (Sigma-Aldrich, Vienna, Austria) and 1 mM of the protease inhibitor phenylmethanesulfonyl fluoride (PMSF, Thermo Fisher Scientific, USA). For protein digestion, the ProtiFi S-trapTM protocol was employed. In short, proteins were reduced and alkylated using dithiothreitol (DTT) and 2-iodoacetamide (IAA), respectively, followed by the addition of trapping buffer (90% v/v methanol, 0.1 M triethylammonium bicarbonate, pH 8.5). Samples were loaded onto S-trapTM cartridges and digested with Trypsin/Lys-C (Promega Corporation, Madison, WI, USA) for 2 h at 37°C. Supernatants containing the digested peptides were eluted, dried, and reconstituted in 5 µL formic acid (FA) containing 10 fmol of four synthetic standard peptides and diluted with 40 µL of mobile phase A (98% H2O, 2% ACN, 0.1% FA). LC-MS/MS measurements were performed on a timsTOF Pro mass spectrometer (Bruker Daltonics) hyphenated with a Dionex UltiMateTM 3000 RSLCnano system (Thermo Fisher Scientific, Austria). The peptide solution (5 µL) was loaded onto an AcclaimTM PepMapTM C18 100 pre-column (Thermo Fisher Scientific, Austria) at a flow rate of 10 µL·min-1 using mobile phase A and eluted onto an Aurora Series emitter column (Ionopticks) applying a flow rate of 300 nL·min-1. Separation was achieved by applying a gradient of 8% to 40% of mobile phase B (80% ACN, 20% H2O, 0.1% FA) over 90 min. For mass spectrometric detection, MS scans were performed from m/z 400–1400 at a resolution of 70,000 (at m/z = 200). All treatments were tested in technical duplicates."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The acquired data was processed using MaxQuant (version 1.6.17.0) with the Andromeda search engine to enable identification and label-free quantification (LFQ) of proteins and searched against the SwissProt homo sapiens database (14.12.2019 with 20380 canonical entries). False discovery rates for peptide-spectrum match (PSM) and protein were set to 0.01. Further criteria included a MS/MS mass tolerance of 40 ppm and a maximum of two missed cleavages. A minimal requirement for protein identification was set to one unique peptide. Carbamidomethylation of cysteine was set as fixed modification while methionine oxidation and the acetylation of the protein N-terminus were included in the search as variable modifications."],"omics_type":["Proteomics"],"labhead":["Christopher Gerner"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["University of Vienna, Faculty of Chemistry, Department of Analytical Chemistry"],"species":["Homo Sapiens (human)"],"publication":["41866874 Iriarte-Mesa C, Juère E, Bileck A, Kremsmayr T, Goodson ML, Ehrlich A, Hodžić A, Kunert M, Gerner C, Kählig H, Marko D, Muttenthaler M, Berry D, Del Favero G, Kleitz F. Mesoporous Silica Nanoparticles-Based Formulations for Enhanced Oral Delivery of Peptide Drugs: A Case Study on Insulin. Small. 2026 22(24):e13347 10.1002/smll.202513347"],"submitter_mail":["christopher.gerner@univie.ac.at"],"submitter_affiliation":["University of Vienna"],"submitter_country":["Austria"],"pubmed_abstract":["Peptide drugs have revolutionized modern medicine owing to their high potency, selectivity, and excellent tolerability. However, oral delivery remains limited, and most peptide drugs are administered parenterally due to their inherent instability to proteolytic digestion and poor ability to cross gastrointestinal barriers, which hinders efficient absorption into the bloodstream. This study presents a multifunctional oral delivery system based on mesoporous silica nanoparticles (MSN) customized for insulin administration. Insulin-loaded MSN were co-formulated with succinylated β-lactoglobulin to produce pH-responsive tablets that limited premature gastric release (≤13% after 2 h at pH 1.2) and protected insulin from enzymatic degradation, while enabling controlled intestinal release (up to 88%-98% at pH 7.4). Surface functionalization with polyethylene glycol and phosphonate moieties improved colloidal stability and increased insulin solubility by ∼2.5-fold. The interaction of phosphonated MSN with intestinal epithelial cells further induced transient reorganization of tight junction proteins, enhancing paracellular insulin transport (26% after 24 h, compared with 13% for non-confined insulin). Delivered insulin retained bioactivity, as demonstrated by activation of insulin-responsive signaling pathways in vitro and reduced blood glucose levels in hyperglycemic mice. These results highlight MSN as a promising platform for oral peptide delivery with improved efficacy and patient compliance."],"pubmed_title":["Mesoporous Silica Nanoparticles-Based Formulations for Enhanced Oral Delivery of Peptide Drugs: A Case Study on Insulin."],"pubmed_authors":["Iriarte-Mesa Claudia C, Juère Estelle E, Bileck Andrea A, Kremsmayr Thomas T, Goodson Michael L ML, Ehrlich Allison A, Hodžić Adnan A, Kunert Martin M, Gerner Christopher C, Kählig Hanspeter H, Marko Doris D, Muttenthaler Markus M, Berry David D, Del Favero Giorgia G, Kleitz Freddy F"],"additional_accession":[]},"is_claimable":false,"name":"Mesoporous Silica Nanoparticles-based Formulations for Enhanced Oral Delivery of Peptide Drugs: a Case Study on Insulin","description":"Peptide drugs have revolutionized modern medicine owing to their high potency, selectivity, and excellent tolerability. However, oral delivery remains limited, and most peptide drugs are administered parenterally due to their inherent instability to proteolytic digestion and poor ability to cross gastrointestinal barriers, which hinders efficient absorption into the bloodstream. This study presents a multifunctional oral delivery system based on mesoporous silica nanoparticles (MSN) customized for insulin administration. Insulin-loaded MSN (MSN(Ins)) were co-formulated with β-lactoglobulin to prevent premature gastric release, enabling delayed controlled intestinal delivery and protecting insulin from degradation. MSN functionalization with polyethylene glycol and phosphonate groups further enhanced MSN colloidal stability and insulin solubility. Phosphonated MSN, in particular, exhibited efficient interactions with intestinal cells, modulating the reorganization of tight junction proteins to promote the paracellular transport of MSN(Ins). Insulin delivered through these formulations retained its activity, as demonstrated by activation of insulin-responsive signaling pathways in vitro and reduction of blood glucose levels in hyperglycemic mice, hallmark responses of insulin treatment in type 2 diabetes. These findings highlight MSN as promising carriers for oral peptide delivery, supporting the development of effective, patient-friendly therapies with enhanced efficacy and 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