Naturally Occurring Peptide Zfra Inactivates Tumor Suppressors by Covalent Binding: An Act of Zfration
Final rept. 1 Sep 2008-31 Aug 2009
NATIONAL CHENG KUNG UNIV TAINAN (TAIWAN)
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In this funded research, we have described zfration - a naturally occurring small-size peptide Zfra undergoes selfcovalent binding and aggregation, and may covalently interact with tumor suppressors for functional inactivation. Zfra is a 31-amino-acid peptide, whose composition is similar to that of zinc finger family proteins. In the original Specific Aims, we proposed to 1 determine how Zfra undergoes covalent self-aggregation and binding with tumor suppressor proteins for regulating their functions 2 determine the overall protein targets with which Zfra interact 3 investigate the effect of Zfra deficiency in breast cancer cells. As research ongoing as planned, we have achieved excellent progress and determined that Zfra can 1 induce degradation of intracellular zfrated proteins, 2 undergo enzyme-independent self-polymerization for more than 200 fold of its original size, and 3 significantly increase the growth of breast and skin basal cell carcinoma in nude mice by 3-4 fold in 3 months, suggestive of its inactivation of tumor suppressors in vivo.
- Medicine and Medical Research
- Inorganic Chemistry