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Mass spectrometry instrumentation continues to evolve rapidly yet quantifying these advances beyond conventional peptide and protein detections remain challenging. Here, we evaluate a modified Orbitrap Astral Zoom mass spectrometer (MS) prototype and compare its performance to the standard Orbitrap Astral MS. Across a range of acquisition methods and sample inputs, the prototype instrument outperformed the standard Orbitrap Astral MS in precursor and protein identifications, ion beam utilization, and quantitative precision. To enable meaningful cross-platform comparisons, we implemented an ion calibration framework that converts signal intensity from arbitrary units to ion per second. This benchmarking strategy showed that the prototype sampled 30% more ions per peptide than the original Orbitrap Astral MS. This increase in the ion beam utilization resulted in improved sensitivity and quantitative precision. To make these metrics broadly accessible, we added new metrics to the Skyline document grid to report the number of ions measured in a spectrum at the apex of the elution peak or the sum of ions between the peak integration boundaries. Taken together, our results demonstrate the prototype Orbitrap Astral Zoom as a high-performance platform for DIA proteomics and establish a generalizable framework for evaluation of mass spectrometer performance based on the number of ions detected for each analyte. Data are available on Panorama Public and on ProteomeXchange under the identifier PXD064536.
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http://dx.doi.org/10.1101/2025.05.30.657132 | DOI Listing |
Sci Data
August 2025
Institute of Advanced Clinical Medicine, Institute of Medical Technology, Peking University Health Science Center, Beijing, China.
Male infertility is fundamentally rooted in developmental defects of germ cells and associated molecular dysregulation, yet the underlying mechanisms remain poorly understood. Data-independent acquisition (DIA) has emerged as a powerful tool in discovery proteomics, enabling the identification of disease biomarkers, therapeutic targets, and molecular pathways with high precision and reproducibility. To analyse the aberrant regulatory events in human sperm proteins associated with male reproductive disorders in a high-throughput, reproducible, and reliable manner, we employed the Orbitrap Astral mass spectrometer, which independently operates Orbitrap Full Scan and Astral MS/MS to generate high-resolution full-scan spectra and high-quality secondary maps.
View Article and Find Full Text PDFChin Med
August 2025
School of Chinese Materia Medica, Beijing University of Chinese Medicine, Beijing, 102488, China.
Background: Acute pharyngitis (AP) is a common upper respiratory tract infection, primarily characterized by symptoms such as throat pain, redness, swelling, and difficulty swallowing. It is typically caused by viral infections, bacterial infections, or physical and chemical irritants. Yuye Jinhua Qingre Tablets (YYJH) are recognized for their ability to clear heat, detoxify, reduce swelling, and alleviate pain, making them a common treatment option for acute pharyngitis.
View Article and Find Full Text PDFMol Cell Proteomics
August 2025
Department for Proteomics and Signal Transduction, Max-Planck Institute of Biochemistry, Martinsried, Germany; Proteomics Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark. Electronic address: mmann@bio
Recent developments in affinity binder or mass spectrometry (MS)-based plasma proteomics are now producing panels of potential biomarker candidates for diagnosis or prognosis. However, clinical validation and implementation of these biomarkers remain limited by the reliance on dated triple quadrupole MS technology. Here, we evaluate a novel hybrid high-speed mass spectrometer, Stellar MS, which integrates the robustness of triple quadrupoles with the enhanced capabilities of an advanced linear ion trap analyzer.
View Article and Find Full Text PDFBackground: Dyslipidemia, marked by elevated LDL-cholesterol (LDL-C), is a major risk factor for coronary heart disease. Mouse models, such as Ldlr-/- mice that develop atherosclerosis and metabolic disorders when fed a high-fat diet (HFD), are indispensable for studying disease mechanisms and identifying potential biomarkers.
Objectives: We aimed to profile the plasma proteins of a widely studied experimental atherosclerosis model with a primary goal to detect low-abundant proteins.
bioRxiv
July 2025
Department of Chemistry and Biochemistry, Brigham Young University, Provo, UT 84602.
Mass spectrometry (MS)-based proteomics remains technically demanding and prohibitively expensive for many large-scale or routine applications, with per-sample costs of hundreds of dollars or more. To democratize access to proteomics and facilitate its integration into more high-throughput multi-omic studies, we present a robust analytical framework for achieving in-depth, quantitative proteome profiling at a cost of approximately $10 per sample, termed the "$10 proteome." Using the Thermo Fisher Orbitrap Astral and Bruker timsTOF Ultra 2 mass spectrometers, we evaluated performance across sample inputs ranging from 200 pg to 100 ng and active gradient lengths from 5 to 60 minutes.
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