PreEMT is a patented technology that employs high pressure for the disaggregation and controlled refolding of proteins to their native structures at yields and efficiencies not achievable using existing technologies. PreEMT results in the dissolution of protein aggregates which may have a significant impact on the quality of protein therapeutics by improving the activity, homogeneity and stability.

BaroFold's technology exposes aggregated protein at any stage in the manufacturing process to elevated pressure, at which water is forced between non-native protein interactions, resulting in disaggregation. The high pressures used by PreEMT forces the protein into its most compact form, usually its native state.  Biologically active, native protein is recovered within hours at yields as high as 100%, even at high protein concentrations.

PreEMT can be applied to a wide variety of therapeutic proteins (existing or novel), including single polypeptide chains, multimeric protein complexes with and without disulfide bridges, and protein crystals.  PreEMT can be utilized in the refolding of recombinant proteins produced in mammalian cells, yeast or E. coli.  PreEMT has significant utility in the refolding of recombinant proteins produced in E. coli at high expression levels as inclusion bodies, most particularly antibody fragments and toxic proteins. In addition, PreEMT may be used to reduce aggregate levels in bulk or final formulations of all classes of therapeutic proteins, thus improving product safety profiles by reducing the risk of aggregate-induced immune responses.

PreEMT is readily scaleable and is practical for the standard manufacturing process for recombinant proteins.  Importantly, PreEMT has the potential to substantially reduce the cost of manufacturing due to its increased efficiency and high yield of refolding.

BaroFold is leveraging PreEMT as a valuable tool to help its industry partners create novel protein therapeutics, accelerate therapeutic protein development, manufacture follow-on biologics, and enable life-cycle management of protein therapeutics.

  • Refolding occurs at conditions that favor the native protein confirmation
  • Aggregates enter the refolding funnel at a lower energy state resulting in:
    • Higher Yields
    • Higher Concentrations (up to 30 mg/ml)
    • Faster Refolding Kinetics
    • No Chaotropes