Encapsulation of proteins in micelles formed via liquid-liquid phase separation (LLPS) is promising method to stabilize proteins of interest, from enzymes to therapeutics. The liquid-liquid phase separation of a globular protein with an ionic block copolymer results in a high density of proteins in the core of the resulting micelle. This highly ionic, hydrated environment stabilizes the protein component during storage, but upon a change in solution pH or ionic strength can release the unmodified protein.<br/><br/>We have evaluated the formation and stability of ionic core micelles with a panel of engineered proteins and neutral-ionic block copolymers. The micelles were characterized by dynamic light scattering and electron microscopy. The impact of polymer properties on protein encapsulation and stability in the micelles has been investigated to determine the optimal design parameters for protein formulation in ionic core micelles.

Ionic core micelles from block copolymers and engineered proteins

256th National Meeting (2018)

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