OCT 24, 2019 9:00 AM PDT

A Comparison of Established NMR Chemometric Methods in Biopharma

C.E. Credits: P.A.C.E. CE Florida CE
Speaker
  • Research Chemist, National Institute of Standards and Technology, Institute for Bioscience and Biotechnology Research
    Biography
      I received a PhD in biochemistry from the University of New Hampshire in 2018 studying biophysical properties of proteins using NMR spectroscopy. I am currently a postdoctoral researcher at the National Institute of Standards and Technology developing analytical NMR spectroscopy methods for assessing the higher order structure of protein therapeutics.

    Abstract

    Therapeutic monoclonal antibodies are a clinically important and life-saving class of biotherapeutics used in the treatment of several previously intractable diseases. However, their development and manufacture presents many significant analytical challenges. The characterization of higher order structure (HOS) is of critical importance, since misfolding or aggregation of a biotherapeutic can lead to loss of efficacy or elicit unintended immune responses. NMR spectroscopy is well suited for such characterization given the ability to detect subtle changes in HOS. Here, we report a combined interlaboratory analysis of 1D and 2D methyl techniques, using linear correlation methods on a panel of mAb samples. Results suggest that the techniques are complimentary to each other, and are reproducible regardless of operator, laboratory and spectrometer field strength.


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