Science of High Pressure Refolding

Protein aggregates generally form through hydrophobic and salt-bridge interactions between chains of a partially or totally unfolded protein. These aggregates may be either soluble or insoluble and form as the result of environmental conditions (temperature, solution conditions, etc.). Aggregation may occur during protein expression in mammalian cell culture, bacculovirus and E. coli, and during routine processing of the protein during manufacturing.

At high hydrostatic pressure, water is forced between the protein molecules causing dissociation of the aggregates. The high pressures used by PreEMT technology forces the protein into its most compact form, usually the native state.