Humanized leucine zipper-TRAIL fusion constructs as potent antitumor agents
OHSU # 2043
Researchers at Oregon Health & Science University have engineered a humanized LZ-TRAIL fusion protein that exhibits potent anti-tumor activity in both cell based and in vivo assays.
Apoptosis induced by chemotherapy and radiotherapy is dependent on the p53 tumor suppressor protein. Many cancer cells do not express p53 and thus are not responsive to such conventional therapies. Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) can induce apoptosis of tumor cells irrespective of the functional status of p53, suggesting that it would be a promising alternative method of targeting tumors that are resistant to conventional therapies.
OHSU researchers previously engineered a yeast leucine zipper (LZ)-human TRAIL chimera in order to improve the half-life, specific activity, and stability of TRAIL. However, this chimera is potentially immunogenic in humans, making it impractical for clinical use. The humanized LZ-TRAIL fusion protein is an improvement over the previous version.
Rozanov D, Spellman P, Savinov A, Strongin AY. A humanized leucine zipper-TRAIL hybrid induces apoptosis of tumors both in vitro and in vivo. 2015: PLoS One, 10(4): e0122980.
This technology is available for licensing.
- Dmitri Rozanov, SM.Molecular & Medical Genetics
|Published||Patent Cooperation Treaty||WO 2016/160576|
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