Investigating Crystalline Protein Suspension Formulations of Pembrolizumab from MAS NMR Spectroscopy
Mingyue Li, Paul Reichert, Chakravarthy Narasimhan, Bradley Sorman, Wei Xu, Aaron Cote, Yongchao Su
Abstract
N spectroscopies have been utilized to identify the binding of caffeine in the pembrolizumab crystal lattice, providing molecular insights into the cocrystallization of the protein and ligand. Our study provides valuable structural details for facilitating the design of crystalline suspension formulation of Keytruda and demonstrates the high potential of MAS NMR as an advanced tool for biophysical characterization of biological therapeutics.
Topics & Concepts
CrystallinityMagic angle spinningChemistryCrystallographyNuclear magnetic resonance spectroscopyChemical engineeringAnalytical Chemistry (journal)Materials scienceChromatographyStereochemistryEngineeringProtein purification and stabilityEnzyme Structure and FunctionProtein Structure and Dynamics