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Related Experiment Videos

Polyethylene glycol enhanced protein refolding.

J L Cleland1, S E Builder, J R Swartz

  • 1Genentech, Inc., S. San Francisco, CA 94080.

Bio/Technology (Nature Publishing Company)
|September 1, 1992
PubMed
Summary

Polyethylene glycol (PEG) enhances protein refolding by reducing aggregation. This study shows PEG significantly improves the recovery of active recombinant human deoxyribonuclease (rhDNAse) and tissue plasminogen activator (rhtPA).

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Area of Science:

  • Biotechnology
  • Protein Chemistry
  • Biochemistry

Background:

  • Recombinant protein refolding is crucial for therapeutic protein production.
  • Protein aggregation during refolding reduces active protein recovery.
  • Polyethylene glycol (PEG) has shown potential in mitigating aggregation.

Purpose of the Study:

  • To evaluate the efficacy of polyethylene glycol (PEG) in enhancing the refolding of recombinant human proteins.
  • To determine optimal PEG concentrations for improved refolding yields.
  • To assess PEG's impact on preventing aggregation during refolding.

Main Methods:

  • Refolding of recombinant human deoxyribonuclease (rhDNAse) and tissue plasminogen activator (rhtPA) in the presence of PEG (3350 MW).
  • Denaturation using urea or guanidine hydrochloride (GuHCl) followed by rapid dilution.

Related Experiment Videos

  • Varying PEG to protein molar ratios in the refolding buffer.

    • Main Results:

    • PEG addition improved rhDNAse refolding by 30% and threefold, depending on purity and PEG ratio.
    • Complete recovery of active rhDNAse was achieved with PEG.
    • PEG addition prevented aggregation of rhDNAse during refolding.
    • rhtPA refolding was initiated using guanidine hydrochloride.

    Conclusions:

    • Polyethylene glycol (PEG) is an effective excipient for enhancing recombinant protein refolding.
    • PEG significantly increases the recovery of active rhDNAse by preventing aggregation.
    • Further studies are warranted for rhtPA and rhIFN-gamma refolding with PEG.