Observation of high-temperature macromolecular confinement in lyophilised protein formulations using terahertz spectroscopy.

ABSTRACT: Characterising the structural dynamics of proteins and the effects of excipients are critical for optimising the design of formulations. In this work we investigated four lyophilised formulations containing bovine serum albumin (BSA) and three formulations containing a monoclonal antibody (mAb, here mAb1), and explored the role of the excipients polysorbate 80, sucrose, trehalose, and arginine on stabilising proteins. By performing temperature variable terahertz time-domain spectroscopy (THz-TDS) experiments it is possible to study the vibrational dynamics of these formulations. The THz-TDS measurements reveal two distinct glass transition processes in all tested formulations. The lower temperature transition, T g , β , is associated with the onset of local motion due to the secondary

SUBMITTER: Shmool TA 

PROVIDER: S-EPMC6733290 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature