Characterization of the physical stability of a lyophilized IgG1 mAb after accelerated shipping-like stress.

ABSTRACT: Upon exposure to shaking stress, an IgG1 mAb formulation in both the liquid and lyophilized state formed subvisible particles. Because freeze-drying was expected to minimize protein physical instability under these conditions, the extent and nature of aggregate formation in the lyophilized preparation were examined using a variety of particle characterization techniques. The effects of formulation variables such as residual moisture content, reconstitution rate, and reconstitution medium were also examined. Upon reconstitution of shake-stressed lyophilized mAb, differences in protein particle size and number were observed by microflow digital imaging, with the reconstitution medium having the largest impact. Shake stress had minor effects on the structure of protein within the particles as

SUBMITTER: Telikepalli S 

PROVIDER: S-EPMC4312241 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature