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Default Characterizing monoclonal antibody formulations in arginine glutamate solutions using (1)H NMR spectroscopy.

Characterizing monoclonal antibody formulations in arginine glutamate solutions using (1)H NMR spectroscopy.

Related Articles Characterizing monoclonal antibody formulations in arginine glutamate solutions using (1)H NMR spectroscopy.

MAbs. 2016 Aug 11;:1-14

Authors: Kheddo P, Cliff MJ, Uddin S, van der Walle CF, Golovanov AP

Abstract
Assessing how excipients affect the self-association of monoclonal antibodies (mAbs) requires informative and direct in situ measurements for highly concentrated solutions, without sample dilution or perturbation. This study explores the application of solution nuclear magnetic resonance (NMR) spectroscopy for characterization of typical mAb behavior in formulations containing arginine glutamate. The data show that the analysis of signal intensities in 1D (1)H NMR spectra, when compensated for changes in buffer viscosity, is invaluable for identifying conditions where protein-protein interactions are minimized. NMR-derived molecular translational diffusion rates for concentrated solutions are less useful than transverse relaxation rates as parameters defining optimal formulation. Furthermore, NMR reports on the solution viscosity and mAb aggregation during accelerated stability study assessment, generating data consistent with that acquired by size-exclusion chromatography. The methodology developed here offers NMR spectroscopy as a new tool providing complementary information useful to formulation development of mAbs and other large therapeutic proteins.


PMID: 27589351 [PubMed - as supplied by publisher]



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