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The SP100 automated liquid-handling robot was used to carry out the entire protocol, from bead incubation and digestion to peptide quantification and peptide reconstitution. Each serum sample was incubated wit two different nanoparticle mixtures, resulting in two fractions per sample (NPA and NPB). After incubation and nanoparticle corona formation, the nanoparticles were separated using a magnetic rack, and unbound components were removed by washing. The proteins bound to the nanoparticles were reduced, alkylated, and digested with trypsin/LysC. The digested peptides were transferred to peptide Clean-up plate. The peptides were washed, filtered and eluted into collection plates under positive pressure (MPE). Peptide quantification was automatically performed using the Pierce Fluorometric Peptide Assay (Thermo Scientific, USA). The peptides were then dried in a SpeedVac. All peptides were resuspended in 2% ACN, 0.1% formic acid in HPLC grade water, and the peptides from NPA and NPB were pooled and injected into the LC-MS/MS. A total of 600 ng of peptides were injected on an Evosep One system coupled to a timsTOF HT (Bruker Daltonics, Germany) mass spectrometer. The Evosep One system operated with 30SPD Samples Per Day (30SPD) using a 15cm x 150µm Performance column (EV1137, Evosep) at 40°C. Mass spectrometric data were acquired using the parallel accumulation serial fragmentation (PASEF) acquisition method in Data Independent Acquisition (DIA) mode with a 19-windows method using 33Da windows covering the mass ranges over a 400-1050m/z. The range of ion mobilities values from 0.67 to 1.29 V s/cm2(1/K0). The cycle time was set to 1.06s."],"repository":["pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The data analysis was performed using DIA-NN software (version 1.8.1) (Demichev et al., 2020). A search against the human UniProtKB/Swiss-Prot Homo sapiens database (downloaded July 03rd 2023, 20423 entries) was performed using the library-free mode. For this purpose, “FASTA digest for library free search/library generation” and “Deep learning spectra, RTs and IMs prediction” options were checked for precursor ion generation. The library-free search parametersincluded digestion with trypsin, tolerating the omission of one cleavage site, and allowing 2 variable modifications. Carbamidomethylation (Cys) was set as the fixed modification, whereas protein N-terminal methionine excision, methionine oxidation and N-terminal acetylation were set as variable modifications. The peptide length range was set to 7-30 amino acids, precursor charge range 2-4, precursor m/z range 300-1800, and a fragment ion range of 200-1800 m/z. The false discovery rates (FDRs) at the protein and peptide level were set to 1%. Match between runs was allowed. For the quantification strategy, Robust LC (high precision) was used as advised in the software documentation, whereas default settings were kept for the other algorithm parameters. Statistical and bioinformatic analysis were performed with Perseus software (version 2.0211) (Tyanova et al., 2016) freely available at www.perseus-framework.org. All protein intensities were log2 transformed to perform statistics. For statistical comparison, we set two groups, each containing 8 biological replicates. We then filtered the data to keep only proteins with 80% valid values in each group. Next, the data were imputed to fill missing data points by creating a Gaussian distribution of random numbers with a standard deviation of 33% relative to the standard deviation of the measured values and 1.8 standard deviation downshift of the mean to simulate the distribution of low signal values. We performed a paired Student’s t-test, FDR<0.05, S0=0."],"omics_type":["Proteomics"],"labhead":["Ida Chiara Guerrera"],"instrument_platform":[""],"labhead_affiliation":["Proteomics Platform Necker, Université Paris Cité - Structure Fédérative de Recherche Necker, INSERM US24/CNRS UAR3633, Paris 75015, France."],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["chiara.guerrera@inserm.fr"],"publication":["10.3389/FPHYS.2026.1773221"],"submitter_affiliation":["Necker proteomics, INSERM"],"submitter_country":["France"],"additional_accession":[]},"is_claimable":false,"name":"Proteograph™-Based Proteome and Sphingolipidome Analysis for Serological Biomarker Discovery in Long-Duration Space Mission","description":"Introduction: Exposure to microgravity for 180 days leads to significant muscle mass and strength loss, which current countermeasures only partially mitigate. This study aimed to identify novel serological biomarkers to monitor muscle tissue adaptations during and after spaceflight. Serum samples from eight astronauts (5 men and 3 women) were collected pre-flight, during flight (IF1, IF2), and post-flight (three days and one month after landing).  Methods: Samples were analyzed using the Proteograph™ XT kit, enabling the detection of protein-level differences before and after flight. Mass spectrometry data were acquired in Data-Independent Acquisition (DIA) mode and analyzed with Perseus software using paired Student’s t-tests, with a false discovery rate (FDR) < 0.05. In addition, sphingolipids were analyzed by targeted mass spectrometry. Results: Among 1,718 detected proteins, 153 showed significant changes, with 11 displaying particularly marked alterations (e.g., PLIN1, PLIN3, and COL11A2), which were validated by immunoblotting. Functional pathway analysis identified ten pathways related to muscle function and cytoskeletal organization, and  one associated with brain function. Moreover, levels of ceramides and sphingomyelins revealed a decrease in total ceramide in the first in-flight sample, followed by a rebound in subsequent samples, accompanied by changes in enzyme levels from muscle extracts.  Conclusion: These findings provide new insights into physiological adaptations to microgravity and identify potential biomarkers for monitoring muscle health during long-duration space 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