Moisture-induced solid state instabilities in alpha-chymotrypsin and their reduction through chemical glycosylation.

ABSTRACT:

Background

Protein instability remains the main factor limiting the development of protein therapeutics. The fragile nature (structurally and chemically) of proteins makes them susceptible to detrimental events during processing, storage, and delivery. To overcome this, proteins are often formulated in the solid-state which combines superior stability properties with reduced operational costs. Nevertheless, solid protein pharmaceuticals can also suffer from instability problems due to moisture sorption. Chemical protein glycosylation has evolved into an important tool to overcome several instability issues associated with proteins. Herein, we employed chemical glycosylation to stabilize a solid-state protein formulation against moisture-induced deterioration in the lyophilized stat

SUBMITTER: Flores-Fernandez GM 

PROVIDER: S-EPMC2924255 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature