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As an absolute method in solution, analytical ultracentrifugation (AUC) enables the quantitative analysis of macromolecules based on their hydrodynamic separation in an applied centrifugal field. These fundamental properties of AUC allow extensive analysis of macromolecules in their native state under biologically relevant conditions and can provide information on their sedimentation coefficients, mass, shape, diffusion coefficients and density. Using gold nanoparticles and the two binding proteins amyloid-beta 42 and BSA, a generally valid procedure for an AUZ-based characterization of ligand-modified nanoparticles is explained with a subsequent quantification of their surface modification by the ligands. Based on the physical-technical fundamentals of AUC, the use of absorption and fluorescence detection systems and the work in the fields of protein and nanoparticle analysis, the broad application possibilities of analytical ultracentrifugation are illustrated and explained.
About the author
Christina Decker, * 1986 in Saarland, studied biomedical engineering and biology in Saarbrücken and Düsseldorf and worked intensively on the use of analytical ultracentrifugation in the field of protein and nanoparticle analysis. She developed a model for calculating the surface binding capacity of nanoparticles.
