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Representative organ-targeted TA-based MPN NPs (i.e., metal free, TA/FeIII-based, TA/TmIII-based, TA/TiIV-based, and TA/GdIII-based) and TiIV-based MPN NPs (i.e., TA/TiIV-based, CAT/TiIV-based, and GA/TiIV-based) were synthesized according to the abovementioned protocol. Equal masses of NP suspension (200 μg per replicate) were mixed with mouse plasma (50 μL) at 2:1 (v/v) and incubated for 15 min to allow the formation of a biomolecular corona on the NP surface. After incubation, the corona-coated MPN NP suspensions were dispersed in 500 μL DPBS and centrifuged (9000 g, 10 min) six times and pellets were redispersed in DPBS (30 μL).      Preparation of plasma proteins for MS analysis   For protein extraction and digestion, proteins from neat plasma and an aliquot (30 μL) of NP suspensions were digested into peptides using S-Trap micro spin columns (ProtiFi, USA #CO2-micro), according to the manufacturer’s protocol.      Briefly, lysis buffer (12 μL, 10% sodium dodecyl sulfate, 100 mM tetraethylammonium bromide (TEAB, pH 8.5) was added to each sample (30 μL), followed by sonication to solubilize proteins. Then, the reducing agent (2 μL, 120 mM tris(2-carboxyethyl)phosphine in water) was added, and the samples were incubated at 55 °C for 15 min. Subsequently, the alkylating agent (2 μL, 500 mM iodoacetamide in 50 mM TEAB) was added and incubated at room temperature for 10 min. Next, acidifier (5 μL, 27.5% phosphoric acid in water) was added, followed by vortexing. To each sample, binding/wash buffer (150 μL, 100 mM TEAB in 90% methanol, pH 7.55) was added and mixed thoroughly. The sample was transferred to an S-Trap micro column placed in a 1.7 mL receiver tube and centrifuged at 4000 g for 30 s to trap proteins. The S-Trap was washed thrice with the binding/wash buffer (150 μL) and centrifugation at 4000 g for 30 s each time. After the final wash, the column was centrifuged at 4000 g for 1 min to completely remove residual buffer. For digestion, the digestion buffer (20 μL, 50 mM TEAB with 2 μg sequencing grade modified trypsin) was added to each column and incubated overnight at 37 °C. To elute peptides, three sequential elutions were performed using the following buffers (40 μL): (1) 50 mM TEAB in water, (2) 0.2% formic acid in water, and (3) 50% acetonitrile in water. After each addition, columns were centrifuged at 4000 g for 1 min. The eluates were pooled and freeze dried. The freeze-dried peptides were resuspended in 2% (v/v) acetonitrile, 0.05% trifluoroacetic acid before analysis by MS.      Liquid chromatography–data-independent acquisition (DIA)–MS was conducted on an Orbitrap Ascend mass spectrometer (Thermo Fisher Scientific) equipped with a nanoflow reversed phase high-performance liquid chromatography system (Ultimate 3000 RSLC, Dionex) fitted with an Acclaim PepMap nano-trap column (Dionex C18, 100 Å, 75 µm × 2 cm) and an Acclaim PepMap RSLC analytical column (Dionex C18, 100 Å, 75 µm × 50 cm). The tryptic peptides were injected to the enrichment column at an isocratic flow of 5 µL min–1 of 2% v/v CH3CN containing 0.1% v/v formic acid for 5 min applied before the enrichment column was switched in-line with the analytical column. The eluents were 5% dimethyl sulfoxide in 0.1% v/v formic acid (solvent A) and 5% dimethyl sulfoxide in 100% v/v CH3CN and 0.1% v/v formic acid (solvent B). The flow gradient was (i) 0–6 min at 3% B, (ii) 6–7 min at 3–4% B, (iii) 7–82 min at 4–25% B, (iv) 82–86 min at 25–40% B, (v) 86–87 min at 40–80% B, (vi) 87–90 min to maintain at 80% B, (vii) 90–90.5 min at 80–3% B and equilibrated at 3% B for 10 min before the next sample injection. For DIA experiments, full MS resolutions were set to 120,000 at m/z 200 and scanning from 350–1400 m/z in profile mode. Full MS automatic gain control target was 250% with an injection time of 50 ms. The automatic gain control target value for fragment spectra was set at 2000%, 50 windows of 13.7 Da were used with an overlap of 1 Da, and the resolution was set to 30,000, maximum IT to 55 ms, and normalized collision energy at 30%. All data were acquired in centroid mode using positive polarity. "],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["Database searching and protein identification   DIA data were analyzed using the direct DIA analysis workflow with default settings on the Spectronaut software (v. 19.4.241104.62635) and against the Mus Musculus database (Uniprot, downloaded Mar 2025). Trypsin specificity was set to two missed cleavages. Carbamidomethyl was defined as fixed modification and acetylation (protein N-term) and oxidation (Met) as variable modification. Results were filtered at a protein and peptide-spectrum match false discovery rate of 1%. Precursor filtering using the q-value and quantification performed on the MS2 level and cross-run normalization strategy set to off. Quantitative data (PG.results) and iBAQ values (PG.IBAQ) were exported for statistical analyses, including correlation plots using the Perseus tool (version 2.0.3.1). iBAQ determines the abundance of a protein by dividing the total precursor intensities by the number of theoretically observable peptides of the protein. The top proteins detected on coronas were determined by percentage intensity based iBAQ values. Three-way and five-way Venn diagrams were generated using the InteractiVenn tool."],"omics_type":["Proteomics"],"labhead":["Frank Caruso"],"instrument_platform":[""],"labhead_affiliation":["Department of Chemical Engineering, The University of Melbourne, Parkville, Victoria 3010, Australia"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"submitter_mail":["yuang.gu1@unimelb.edu.au"],"publication":["Not available"],"submitter_affiliation":["Department of Chemical Engineering, The University of Melbourne, Parkville, Victoria 3010, Australia"],"submitter_country":["Australia"],"additional_accession":[]},"is_claimable":false,"name":"Selective organ deposition of nanoparticles directed by metal–organic network coatings_2","description":"Despite significant advances in nanoengineering, developing a universal nanoparticle engineering strategy that enables tailored nanoparticle organ deposition post intravenous administration remains challenging. Here, we report a simple and modular strategy mediated by metal–organic network coatings composed of polyethylene glycol (PEG), proteins, phenolic ligands, and metal ions. The versatile binding affinity of phenolic ligands facilitates the formation of coatings on diverse nanoparticle platforms, including quantum dots, lipid, polymeric, inorganic, and metal–organic nanoparticles. The organ deposition selectivity of these coated nanoparticles is readily directed towards the kidney, lung, heart, and brain by varying the coating composition. Mechanistic studies reveal that the combined effect of PEG, phenolic ligands, and metal ions on the surface properties governs the overall biodistribution of the coated nanoparticles, while the protein component contributes to the coating integrity. This work provides a generalizable approach for developing an organ-targeting nanotechnology, with the potential to advance nanoparticle-mediated treatments and theranostics.","dates":{"publication":"2026-06-26","submission":"2026-04-27"},"accession":"PXD077631","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:111205","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:383379","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:317447","NEWT:4688","NEWT:111225","NEWT:7719","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:160621","NEWT:212790","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:5507","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:3702","NEWT:1245466","NEWT:244366","NEWT:1246791","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2853422","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:109760","NEWT:29031","NEWT:235443","NEWT:108458","NEWT:5936","NEWT:320637","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:1255228","NEWT:410289","NEWT:373153","NEWT:472","NEWT:1071661","NEWT:470","NEWT:5911","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:575412","NEWT:28112","NEWT:6493","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:8655","NEWT:5147","NEWT:28104","NEWT:407821","NCBITaxon:2","NEWT:568708","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:40674","NEWT:1194669","NEWT:51329","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:6063","NEWT:1328388","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:80863","NEWT:90675","NEWT:52638","NEWT:57075","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:1123869","NEWT:9544","NEWT:9545","NEWT:979","NEWT:7370","NEWT:83906","NEWT:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:305959","NEWT:92867","NEWT:92866","NCBITaxon:3055","NEWT:51750","NEWT:202950","NEWT:295027","NCBITaxon:11320","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:90690","NEWT:1436183","NEWT:4232","NEWT:416348","NEWT:11298","NEWT:196627","NEWT:200308","NEWT:200302","NEWT:870435","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:2666255","NEWT:999810","NCBITaxon:5693","NEWT:28995","NEWT:1392998","NEWT:380394","NEWT:226900","NEWT:1266738","NEWT:231490","NEWT:244704","NEWT:7725","NEWT:430615","NEWT:563041","NEWT:72664","NEWT:326423","NEWT:452467","NEWT:198822","NEWT:36111","NEWT:326424","NEWT:1678078","NEWT:749906","NEWT:418985","NEWT:749907","NEWT:150847","NEWT:431947","NEWT:69014","NEWT:142809","NEWT:302409","NEWT:130821","NEWT:27606","NEWT:1519788","NEWT:59202","NEWT:9975","NEWT:8643","NEWT:1159899","NEWT:502780","NEWT:860688","NEWT:13443","NEWT:8644","NEWT:5141","NEWT:46360","NCBITaxon:3044782","NEWT:20291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