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Decoupling Protein Concentration and Aggregate Content Using Diffusion and Water NMR.

Mark I Grimes1, Matthew Cheeks2, Jennifer Smith2

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Water NMR (wNMR) can now separate protein concentration and aggregate levels. By measuring water diffusion (D) alongside relaxation rates (R2), this method offers a new tool for bioprocess monitoring.

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Area of Science:

  • Biopharmaceutical analysis
  • Process Analytical Technology (PAT)
  • Nuclear Magnetic Resonance (NMR) spectroscopy

Background:

  • Protein-based drugs, like monoclonal antibodies, are leading global pharmaceuticals.
  • Monitoring protein concentration and aggregate levels is crucial for bioprocess control.
  • Water NMR (wNMR) using transverse relaxation rate (R2) can measure protein concentration and aggregates but cannot distinguish between them.

Purpose of the Study:

  • To develop a method to "decouple" and simultaneously determine protein concentration and aggregate levels in biopharmaceuticals.
  • To overcome the limitations of existing wNMR techniques that cannot differentiate these two critical parameters.

Main Methods:

  • Utilized water diffusion coefficient (D(H2O)) measurements in conjunction with water transverse relaxation rate (R2(H2O)) from wNMR.
  • Demonstrated the method on three different protein systems.
  • Involved calibration data acquisition for D(H2O) and R2(H2O) specific to the protein of interest.

Main Results:

  • Successfully decoupled and determined both protein concentration and aggregate levels simultaneously.
  • The combined D(H2O) and R2(H2O) approach works even when individual parameters overlap.
  • Validated the method across diverse protein systems.

Conclusions:

  • The combined wNMR approach (D(H2O) + R2(H2O)) effectively separates protein concentration and aggregate levels.
  • This technique shows promise for implementation as an at-line process analytical technology.
  • Enables more precise bioprocess monitoring and control for protein-based therapeutics.