Using Solid-State NMR Spectroscopy as a Tool for Developing Stable Lyophilized Protein Formulations

Solid-State Nuclear Magnetic Resonance Spectroscopy (SSNMR) is a powerful analytical tool that can be utilized in order to characterize the lyophilized matrix and predict stability in lyophilized protein formulations. SSNMR can access different length scales and time scales in the solid matrix. Using 1H T1 and 1H T1rho relaxation times, phase separation can be studied on 20-50 nm and 2-5 nm length scales. The 1H T1 relaxation time can also access the ps-ns timescale, which provides information on the local mobility within the cake matrix. This webinar will provide several case studies focusing on the analysis of phase separation and local mobility using SSNMR in formulations containing various proteins (lysozyme, BSA, and IgG) and stabilizers (sucrose, trehalose, and mannitol). Additionally, a study using SSNMR to study ionization changes in the solid matrix will be presented.

Presented by Ashley Lay-Fortenbery, PhD Candidate in Pharmaceutical Sciences at the University of Kentucky College of Pharmacy