ArticleJournal of the American Society for Mass Spectrometry2025
Characterizing the Content and Structure of AAV Capsids by Size Exclusion Chromatography and Orbitrap-Based Charge Detection-Mass Spectrometry.
Article in Journal of the American Society for Mass Spectrometry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
4 citing papers in PubMed.
- Modulating pressure in the Orbitrap improves sensitivity and mass resolution in charge detection mass spectrometry.Nature communications · 2026Article
- Native Multidimensional Protein Complex Identification and Topology Characterization (Native MudPIT).Analytical chemistry · 2026Article
- Sheath-Liquid CE-MS Interface: A Robust Infusion Platform for Native IMS-MS Analysis of Protein Assemblies and Their Conformers.Journal of mass spectrometry : JMS · 2026Article
- Development of a gene-activated matrix for enhanced AAV gene deliveryFrontiers in bioengineering and biotechnology · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
Abstract
Adeno-associated virus (AAV) is currently the most widely used vector in gene therapy applications. However, a significant challenge in the manufacturing process of recombinant AAV (rAAV) is the presence of empty capsids, oligomers, aggregates, and partially filled capsids. These components do not provide any therapeutic benefit but add to the overall viral load, which could increase immunogenicity and reduce transduction efficiency. Here, we present a strategy that utilizes size exclusion chromatography (SEC) equipped with multiangle light scattering (MALS) and a diode-array detector (DAD), followed by orbitrap-based charge detection-mass spectrometry (CD-MS). The SEC step was used to separate AAV capsids (non-aggregates) from oligomers, aggregates, and low molecular weight contaminants. In the second step, we employed direct CD-MS infusion using capillary electrophoresis with a sheath liquid (MS) interface. This approach facilitated automated, reproducible, sensitive, and robust CD-MS determination of empty-filled capsids, capsid oligomers, and encapsidated genomes. Importantly, the empty-to-filled capsid ratio was inaccurate without the SEC step. Together, our analytical platform offers a reliable and comprehensive approach for assessing the rAAV purity and characterizing key quality attributes, including capsid aggregation, capsid oligomerization, and genome packaging.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.