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- W2334773060 endingPage "575" @default.
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- W2334773060 abstract "We have investigated the effects of site specific “hinge” polyethylene glycol conjugation (PEGylation) on thermal, pH, and colloidal stability of a monoclonal antibody antigen-binding fragment (Fab′) using a variety of biophysical techniques. The results obtained by circular dichroism (CD), ultraviolet (UV) absorbance, and fluorescence spectroscopy suggested that the physical stability of the Fab′ is maximized at pH 6–7 with no apparent differences due to PEGylation. Temperature-induced aggregation experiments revealed that PEGylation was able to increase the transition temperature, as well as prevent the formation of visible and subvisible aggregates. Statistical comparison of the three-index empirical phase diagram (EPD) revealed significant differences in thermal and pH stability signatures between Fab′ and PEG-Fab′. Upon mechanical stress, micro-flow imaging (MFI) and measurement of the optical density at 360 nm showed that the PEG-Fab′ had significantly higher resistance to surface-induced aggregation compared to the Fab′. Analysis of the interaction parameter, kD, indicated repulsive intermolecular forces for PEG-Fab′ and attractive forces for Fab′. In conclusion, PEGylation appears to protect Fab′ against thermal and mechanical stress-induced aggregation, likely due to a steric hindrance mechanism." @default.
- W2334773060 created "2016-06-24" @default.
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- W2334773060 date "2015-01-14" @default.
- W2334773060 modified "2023-09-30" @default.
- W2334773060 title "Effect of Polyethylene Glycol Conjugation on Conformational and Colloidal Stability of a Monoclonal Antibody Antigen-Binding Fragment (Fab′)" @default.
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- W2334773060 doi "https://doi.org/10.1021/mp500658w" @default.
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