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Protein improves efficacy of tumor-killing enzyme
Date:4/29/2013

he wild-type ubiquitin or engineered ubiquitin without lysine residues in it, a change that should prevent it from being degraded by the cell. The addition of ubiquitin enhanced the ability of the PEIII enzyme to persist inside the cell thereby enhancing its potency. And the ubiquitin didn't seem to hinder the efficiency of delivering the PEIII inside the cell.

As an added bonus, the addition of ubiquitin reduced the toxicity of the targeted toxin to non-tumor tissues.

The authors point out that the use of ubiquitin linkers shows considerable promise and could be an effective strategy for enhancing the potency of tumor-targeting toxins for use in patients. In research currently underway, they are attempting to improve on the system by making changes to the ubiquitin that allow it to unfold appropriately inside the cell.


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Contact: Jim Sliwa
jsliwa@asmusa.org
202-942-9297
American Society for Microbiology
Source:Eurekalert

Page: 1 2

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