Analytical Ultracentrifugation (AUC) is one
of the main technical means to characterize the characteristics of
biomacromolecules and study the physicochemical properties of biomolecules. It
is used to analyze sample heterogeneity, aggregate formation, and intermolecular
interactions. The Swedish scientist Theodor Svedberg invented the technology in
1925 and built the first analytical ultracentrifuge
the following year. After nearly a hundred years of application, verification,
and development, this technology has been widely used in research fields such
as biopharmaceuticals, life sciences, and polymer sciences.
The analytical methods of analytical
ultracentrifugation mainly include sedimentation velocity (Sedimentation
Velocity) and sedimentation equilibrium (Sedimentation Equilibrium).
Settling rate is a hydrodynamic technique. In the sedimentation rate experiment,
the sample is rotated at a high speed, the solute molecules move toward the
bottom of the sample cell, and the rate of the solute molecule movement is
measured by the recorded data. The rate of movement is expressed by the
sedimentation coefficient, which depends on molecular weight, molecular shape,
or conformation. For samples of different components, each component is
detected according to different sedimentation coefficients.
Settling equilibrium is a thermodynamic
technique. The sedimentation equilibrium test was carried out at a low
rotational speed, and the distribution of molecular equilibrium concentration
was determined when the sedimentation and diffusion reached equilibrium. In
equilibrium, the distribution of concentration depends only on the mass and not
on the shape of the molecule. At the beginning of centrifugation, the molecular
particles settle. After a period of time, the sedimentation results in a
concentration gradient, thus resulting in the reverse diffusion of protein
molecules. When the reverse diffusion and centrifugal sedimentation reach
equilibrium, the concentration distribution remains unchanged.
After the sedimentation data is obtained by
scanning, the sample characterization results can be obtained through
subsequent software analysis. At present, SEDFIT/SEDPHAT analysis software is
widely used. According to the analysis results, the aggregation state of
biological macromolecules and the accurate percentage content of aggregates can
be accurately detected. Analytical ultracentrifugation technology has its
unique advantages in the detection of protein drug aggregates. It does not
require standards and markers, and directly detects the state of the sample in
the final solution, which is closer to the real physiological state of the
protein.
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