{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077140/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077140/25-12-01_AST1-25-3983_Naser_P25-2724.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077140/25-12-01_AST1-25-3981_Naser_P25-2722.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077140/25-12-01_AST1-25-3987_Naser_P25-2728.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077140/25-12-01_AST1-25-3985_Naser_P25-2726.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077140/25-12-01_AST1-25-3990_Naser_P25-2731.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077140/25-12-01_AST1-25-3992_Naser_P25-2733.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077140/25-12-01_AST1-25-3994_Naser_P25-2735.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077140/25-12-01_AST1-25-3982_Naser_P25-2723.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077140/25-12-01_AST1-25-3980_Naser_P25-2721.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077140/25-12-01_AST1-25-3988_Naser_P25-2729.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077140/25-12-01_AST1-25-3986_Naser_P25-2727.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077140/25-12-01_AST1-25-3984_Naser_P25-2725.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077140/25-12-01_AST1-25-3979_Naser_P25-2720.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077140/25-12-01_AST1-25-3995_Naser_P25-2736.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077140/25-12-01_AST1-25-3991_Naser_P25-2732.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077140/25-12-01_AST1-25-3993_Naser_P25-2734.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077140/26-03-30_Rawfile_names_EN.ods"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["b.haeupl@dkfz-heidelberg.de"],"submitter":["Josefine Jakob"],"technology_type":["Mass Spectrometry","Data-independent acquisition","Bottom-up proteomics"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077140"],"tissue":["Blood Serum"],"sample_protocol":["For LC/MS analysis, 5 μl plasma or amyloid extracts from abdominal fat aspiration were mixed with 15 μl of denaturing buffer (20 mM HEPES pH 8.5, 4% SDS, 0.2% Na-Deoxycholate, 50 mM TCEP) and incubated for 60 min at 55°C.  Protein concentrations of the lysates were determined using the 660 nm assay kit (Thermo Fisher Scientific) according to the manufacturer’s instructions. The samples were alkylated using iodoacetamide in a final concentration of 50 mM for 30 min at room temperature in the dark. 80 μg of protein were purified and digested using a SP3 protocol based on magnetic beads (Hughes et al., 2019, https://doi.org/10.1038/s41596-018-0082-x ). For this, 50 mg/ml E3 and E7 carboxylate beads (Cytiva) were mixed 1:1, washed 2x with water and added to the samples in a 10:1 bead-to-protein ratio. To induce binding of proteins to the beads, acetonitrile (ACN) was added to a final concentration of 50% and the mixtures were incubated for 60 min at 24°C and 1000 rpm. The samples were centrifuged 2 min at 5000 xg, placed on a magnetic rack and the supernatant was removed. The beads were then washed 2x with 80% ethanol and 1x with 100% ACN. After the last washing step, the beads were air-dried and resuspended in 100 μl 50 mM TEAB containing LysC (Wako) in a 1:50 enzyme-to-protein ratio and incubated for 2 h at 37°C. Afterwards, trypsin (Promega) was added (1:50) and the samples were incubated for 18 h at 37°C with shaking. The samples were centrifuged for 2 min at 5000 xg, placed on a magnetic rack and the supernatant was transferred to a fresh protein low-bind tube. To complete the elution, 30 μl water were added to the beads, they were sonicated for 60 seconds and the supernatant was added to the eluate. Finally, the samples were vacuum dried and peptides were resuspended in 0.1% FA. Peptide concentrations were determined using a fluorometric peptide assay (Thermo Fisher Scientific). The peptide samples were analyzed by LC-MS/MS on a Vanquish Neo UHPLC system coupled online to an Orbitrap Astral mass spectrometer (both Thermo Fisher Scientific) using a data-independent acquisition scheme (DIA). Per run, 200 ng of peptides were concentrated and desalted on a PepMap Neo C18 trap cartridge (pore size 100 Å, particle size 5 µm, inner diameter 300 μm, length 5 mm, Thermo Fisher Scientific), followed by separation on a 25 cm Aurora C18 analytical column (pore size 120 Å, particle size 1.7 µm, inner diameter 75 µm, IonOpticks) using a 25 min method with a 19.5 min linear gradient of 2% to 40% solvent B (0.1% FA in 99.9% ACN) over solvent A (0.1% FA) at a flow rate of 400 nL/min. Precursor and fragment ion scans in the Orbitrap and the Astral mass analyzer, respectively, were performed using the same acquisition method and settings as described previously in Stahl et al., 2025 (https://www.cell.com/cancer-cell/fulltext/S1535-6108(25)00222-3)."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Raw DIA data were analyzed using Proteome Discoverer (version 3.1.1.93, Thermo Fisher Scientific) using the CHIMERYS search algorithm. The mass spectra were searched against the Uniprot human reference proteome (release 05-2024) and 245 frequently observed contaminants and additionally, individual LC sequences were included in the database. Further data processing was done using R studio (version 2024.09.1). Potential contaminants were removed and to control for equal sample loading, intensities from each LC-MS/MS run were normalized on the median of the summed-up intensities from each sample."],"omics_type":["Proteomics"],"labhead":["Björn Häupl"],"instrument_platform":[""],"labhead_affiliation":["Department of Medicine II, Hematology/Oncology, Goethe University, Frankfurt, Germany. German Cancer Research Center (DKFZ) and German Cancer Consortium (DKTK), Heidelberg, Germany."],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["j.jakob@med.uni-frankfurt.de"],"publication":["Not available"],"submitter_affiliation":["Frankfurt Cancer Institute (FCI), Goethe University, Frankfurt, Germany\nDepartment of Medicine II, Hematology/Oncology, Goethe University, Frankfurt, Germany"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"RNA-based full length immunoglobulin light chain sequencing reveals lambda constant domain mutations with potential implications for thermodynamic stability in light chain amyloidosis","description":"Background: Systemic light chain amyloidosis is a protein misfolding disorder characterized by deposition of clonal immunoglobulin light chains in vital organs. To date, little is known about the contribution of light chain constant domain mutations in thermodynamic stability and amyloidogenicity.Methods: In 89 patients, RNA-based full-length light chain repertoire sequencing with Oxford Nanopore was performed, in addition to Illumina sequencing and mass spectrometric detection of light chain protein in serum and amyloid deposits. Computational methods for conservation, free energy calculation, and molecular dynamics simulations were applied to investigate the thermodynamic stability.Results: Monoclonal light chain detection rate was 95.4%, and sequences showed 100% identity with Illumina in all patients. Light chain protein was specifically detectable by mass spectrometry in serum and amyloid deposits. Lambda constant domain mutations were present in 10%, while no kappa constant domain mutations were detected. Fold free energy change and molecular dynamics simulations indicate potential light chain stabilizing or destabilizing effects of detected constant domain mutations.Conclusion: Current findings highlight the importance of routinely implementing full-length light chain sequencing in plasma cell dyscrasias, particularly light chain amyloidosis to account for the potential impact of constant domain mutations on light chain stability and 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