@entity2625 formation in XXXX 80 and protein stability.

@entity2627 @entity6496 @entity26 @entity2625 @entity2041 @entity1199 @entity9266
Nonionic surfactants are widely used in the development of protein pharmaceuticals. However, the low level of residual @entity2627 in surfactants can potentially affect the stability of oxidation-sensitive proteins. In this report, we examined the @entity2625 formation in @entity6496 80 under a variety of storage conditions and tested the potential of @entity2627 in @entity6496 80 to oxidize a model protein, @entity1199 mutein. For the first time, we demonstrated that @entity2627 can be easily generated in neat @entity6496 80 in the presence of air during incubation at elevated temperatures. @entity6496 80 in aqueous solution exhibited a faster rate of @entity2625 formation and a greater amount of @entity2627 during incubation, which is further promoted/catalyzed by light. @entity2625 formation can be greatly inhibited by preventing any contact with air/ @entity26 during storage. @entity1199 mutein can be easily oxidized both in liquid and solid states. A lower level of @entity2627 in @entity6496 80 did not change the rate of @entity1199 mutein oxidation in liquid state but significantly accelerated its oxidation in solid state under air. A higher level of @entity2627 in @entity9266 caused a significant increase in @entity1199 mutein oxidation both in liquid and solid states, and @entity2041 can significantly inhibit the @entity2625 -induced oxidation of @entity1199 mutein in a lyophilized formulation. In addition, a higher level of @entity2627 in @entity6496 80 caused immediate @entity1199 mutein oxidation during annealing in lyophilization, suggesting that implementation of an annealing step needs to be carefully evaluated in the development of a lyophilization process for oxidation-sensitive proteins in the presence of @entity6496 .
