Protein storage with perfluorinated PEG compartments in a hydrofluorocarbon solvent

We report a novel storage technology of proteins with surface-perfluorinated poly(ethylene glycol) compartments in 2H, 3H-perfluoropentane. The compartments were obtained from self-folding and self-assembly of an amphiphilic random copolymer bearing poly(ethylene glycol) and perfluoroalkyl pendants in the hydrofluorocarbon. Lysozyme and alpha-chymotrypsin as model proteins were efficiently encapsulated within the PEG compartments and quantitatively recovered therefrom with water. The recovered lysozyme maintained the original higher order structure without denaturation to show enzymatic activity for the hydrolysis of Micrococcus lysodeikticus as high as its original counterpart in water. The storage technology was further effective to inhibit inactivation of alpha-chymotrypsin.