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Determining Spectroscopic Quantitation Limits for Misfolded Structures.

Brent S Kendrick1, John P Gabrielson1, Caroline Warly Solsberg1

  • 1KBI Biopharma, Inc., Louisville, Colorado 80027.

Journal of Pharmaceutical Sciences
|September 16, 2019
PubMed
Summary
This summary is machine-generated.

This study assessed spectroscopic methods for detecting protein misfolds. Circular dichroism and infrared spectroscopy showed promise in quantifying structural impurities during drug development.

Keywords:
Fourier transform infrared (FTIR)analytical biochemistrybiopharmaceutical characterizationbiosimilarscircular dichroismspectroscopy

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Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Pharmaceutical Sciences

Background:

  • Protein secondary structure analysis is crucial in pharmaceutical development, particularly for monoclonal antibodies.
  • Current spectroscopic methods lack defined lower limits for quantifying structural misfolds and impurities.
  • Ensuring protein structural integrity is vital for drug safety and efficacy.

Purpose of the Study:

  • To evaluate the sensitivity and quantitation capabilities of different spectroscopic techniques for detecting protein structural misfolds.
  • To establish the lower limits of quantitation for impurities with distinct secondary structures.
  • To assess the utility of spectral comparison algorithms in identifying and quantifying misfolded proteins.

Main Methods:

  • A model system using monoclonal antibody reference material spiked with a protein exhibiting a different secondary structure was employed.
  • Circular dichroism (CD) spectroscopy, transmission Fourier transform infrared (FTIR) spectroscopy, and microfluidic modulation spectroscopy (MMS) were utilized.
  • Various spectral comparison algorithms were applied to analyze the data.

Main Results:

  • The study determined the lower limits of quantitation for detecting and quantifying structural misfolds using the assessed spectroscopic methods.
  • Circular dichroism and FTIR spectroscopy demonstrated potential for quantifying misfolded structures.
  • The effectiveness of spectral comparison algorithms in identifying structural variations was evaluated.

Conclusions:

  • Spectroscopic methods, including CD and FTIR, can be employed to detect and quantify protein structural misfolds in pharmaceutical development.
  • Further investigation into spectral comparison algorithms can enhance the accuracy of impurity quantification.
  • Establishing lower limits of quantitation is essential for robust comparability and biosimilarity studies.