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A simplified method for the efficient purification and refolding of recombinant human TRAIL
Zhenjiang Zhang1, Su Bin Hahn1, Thong M Cao1
1Department of Biomedical Engineering, Vanderbilt University, Nashville, TN, USA.
Biotechnology Progress
|April 25, 2020
Summary
Recombinant human TRAIL (rhTRAIL) can induce cancer cell death but is difficult to produce. This study presents a simplified method for high-yield production of pure, bioactive rhTRAIL from E. coli inclusion bodies.
Area of Science:
- Biochemistry
- Molecular Biology
- Oncology
Background:
- Tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) is a protein with significant antitumor potential.
- TRAIL induces apoptosis in cancer cells while sparing healthy cells.
- Expressing recombinant human TRAIL (rhTRAIL) in E. coli often leads to low yields of active protein due to inclusion body formation.
Purpose of the Study:
- To develop a simplified and efficient method for producing pure, bioactive rhTRAIL in E. coli.
- To overcome the challenge of inclusion body formation during rhTRAIL expression.
Main Methods:
- Utilized a simplified protocol for rhTRAIL production in E. coli.
- Focused on efficient purification and renaturation of proteins from inclusion bodies.
Main Results:
- Achieved high yields of pure and bioactive rhTRAIL.
- The method is straightforward, requiring only basic laboratory equipment.
- Demonstrated high efficiency in purification and renaturation.
Conclusions:
- A highly simplified method for producing pure, bioactive rhTRAIL from E. coli inclusion bodies has been established.
- This method offers high yield, efficient purification, and successful renaturation.
- The technique may be applicable to the production of other proteins that form inclusion bodies.
