Conformational jamming of protein molecules in the solid state measured by terahertz dynamics

Описание: Johanna Kölbel, a third year PhD student from the group, is presenting a talk for the 45th International Conference on Infrared, Millimeter, and Terahertz Waves - a virtual event this year due to the coronavirus pandemic. She shows how terahertz spectroscopy can be used as a new tool to optimise the protein stability in biopharmaceutical formulations.

Johanna is a student with the EPSRC Sensor CDT (https://cdt.sensors.cam.ac.uk) and her work is co-funded by AstraZeneca. In this study she shows some of her results from a recent collaboration with the group of Wolfgang Frieß from the Department of Pharmacy, Pharmaceutical Technology and Biopharmaceutics at the Ludwig-Maximilians-University, Munich, Germany (https://www.cup.lmu.de/pb/aks/friess/).



Stability of Protein-Sugar Lyophilisates Investigated with Terahertz Spectroscopy
J. Kölbel , M. L. Anuschek , I. Seifert , W. Frieß and J. A. Zeitler

Understanding of the molecular mobility in freeze-dried matrices is of high importance for the assessment and prediction of the stability of lyophilised protein and peptide drugs. Using terahertz spectroscopy it is possible to measure the molecular mobility in such lyophilisates. Here we analyse samples composed of different ratios of the excipient sucrose to monoclonal antibody (mAb). Upon increasing the relative amount of mAb in the mixture we observe evidence for vibrational confinement which clearly originates from the protein molecules and not the excipient matrix or residual water molecules in the system.