ArticleAnalytical and bioanalytical chemistry2023
Realizing the AF4-UV-SAXS on-line coupling on protein and antibodies using high flux synchrotron radiation at the CoSAXS beamline, MAX IV.
Article in Analytical and bioanalytical chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- Resolving Heterogeneity of Targeted Lipid Nanoparticles Through Solution-Based Biophysical Analyses.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Structural Profiling of Lipid Nanoparticles at Sub-10 nm Resolution via AF4 Coupled Online to SAXS and SANS.Small methods · 2026Article
- Resolving heterogeneity of targeted lipid nanoparticles through solution-based biophysical analyses.bioRxiv : the preprint server for biology · 2026Article
- Structural heterogeneity in mRNA-LNP subpopulations revealed by AF4-SAXS: implications for cargo loading and cell transfection.bioRxiv : the preprint server for biology · 2026Article
- AF4-to-SAXS: expanded characterization of nanoparticles and proteins at the P12 BioSAXS beamline.Journal of synchrotron radiation · 2025Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
In this paper, we demonstrate the coupling of synchrotron small angle X-ray scattering (SAXS) to asymmetrical flow-field flow fractionation (AF4) for protein characterization. To the best of our knowledge, this is the first time AF4 is successfully coupled to a synchrotron for on-line measurements on proteins. This coupling has potentially high impact, as it opens the possibility to characterize individual constituents of sensitive and/or complex samples, not suited for separation using other techniques, and for low electron density samples where high X-ray flux is required, e.g., biomolecules and biologics. AF4 fractionates complex samples in native or close to native environment, with low shear forces and system surface area. Many orders of magnitude in size can be fractionated in one measurement, without having to reconfigure the experimental setup. We report AF4 fractionations with correlated UV and statistically adequate SAXS data of bovine serum albumin and a monoclonal antibody and evaluate SAXS data recorded for the two protein systems.
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Registered trials
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