Characterization of Protein Higher Order Structure Using Vibrational Circular Dichroism Spectroscopy
2013
Better understanding of protein higher order structures (HOS) is of major interest to researchers in the field of
biotechnology and biopharmaceutics. Monitoring a protein’s HOS is crucial towards understanding the impact of molecular
conformation on the biotechnological application. In addition, maintaining the HOS is critical for achieving robust
processes and developing stable formulations of therapeutic proteins. Loss of HOS contributes to increased aggregation,
enhanced immunogenicity and loss of function. Selecting the proper biophysical methods to monitor the secondary and
tertiary structures of therapeutic proteins remains the central question in this field. In this study, both Fourier Transform
Infrared (FTIR) and vibrational circular dichroism (VCD) spectroscopy are employed to characterize the secondary structures
of various proteins as a function of temperature and pH. Three proteins with different secondary structures were examined,
human serum albumin (HSA), myoglobin, and the monoclonal antibody, ofatumumab. This work demonstrates
that VCD is useful technique for monitoring subtle secondary structure changes of protein therapeutics that may occur
during processing or handling.
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