Aggregation of anti-streptavidin immunoglobulin gamma‐1 involves Fab unfolding and competing growth pathways mediated by pH and salt concentration
N Kim, RL Remmele Jr, D Liu, VI Razinkov… - Biophysical …, 2013 - Elsevier
Changes in non-native aggregation mechanisms of an anti-streptavidin (anti-SA) IgG1
antibody were determined over a wide range of pH and [NaCl] under accelerated (high
temperature) conditions, using a combination of calorimetry, chromatography, static light
scattering, dye binding, and spectroscopy (fluorescence, infra-red, and circular dichroism).
Aggregation rates were strongly influenced by conformational stability of at least the Fab
regions, but were only weakly affected by changes in electrostatic colloidal interactions. This …
antibody were determined over a wide range of pH and [NaCl] under accelerated (high
temperature) conditions, using a combination of calorimetry, chromatography, static light
scattering, dye binding, and spectroscopy (fluorescence, infra-red, and circular dichroism).
Aggregation rates were strongly influenced by conformational stability of at least the Fab
regions, but were only weakly affected by changes in electrostatic colloidal interactions. This …
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