Abstract
Spectral similarity supports comparison of circular dichroism (CD) spectra by using all datapoints to improve alignment of wavelength, intensity and offset. CD is increasingly used to confirm the higher order structure and stability of biopharmaceutical proteins, which requires method validation and assessment of robustness in quality regulated analytical systems. Camphor-10-sulphonic acid (CSA), or its ammonium salt, is widely used to calibrate spectropolarimeters, with its use specified in the European Pharmacopoeia (EP), and, more broadly, as a system suitability standard. Spectral similarity comparison of 75 CSA reference spectra in the Protein Circular Dichroism Data Bank (PCDDB) showed the potential value of this approach to monitor instrument performance and support compliance within a quality system.
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