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Eliminating the six N-terminal amino acids of the Caspase 3 large subunit improved production of a biologically active IL2-Caspase3 chimeric protein.
Author: Glantz, Y., Sabag, O., Lichtenstein, M., Grodzovski, I., Lorberboum-Galski, H.
Source: Biotechnol Prog, , 10.1002/btpr.1515
Abstract: Designing a chimeric protein and developing a procedure for its stable production as a biologically active protein, are key steps in its potential application to clinical trails. IL2-Caspase3 chimeric protein designed to target activated T lymphocytes was found to be a promising molecule for targeted treatment, however was found to be difficult to produce as a biological active molecule. Thus, we designed a new version of the molecule, IL2-Caspase3s, in which six amino acids (a.a. 29-34) from the N-terminus of the large subunit of caspase 3 were excluded. Repeated expressions, productions and partial purifications of the IL2-Caspase3s yielded reproducible batches with consistent results. We found that IL2-Caspase3s causes cell death in a specific, dose and time dependent manner. Cell death due to IL2-Caspase3s is caused by apoptosis. This improved and biologically stable IL2-Caspase3s chimeric protein may be developed in the future for clinical trails as a promising therapy for several pathologies involving activated T-cells. Moreover, this truncated Caspase 3 sequence, lacking the N-terminal six amino acids of its large subunit, may be used in other Caspase 3-based chimeric proteins targeted against various human diseases, using the appropriate targeting moiety. © 2011 American Institute of Chemical Engineers Biotechnol. Prog., 2011.
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