Naturally Occurring Peptide Zfra Inactivates Tumor Suppressors by Covalent Binding: An Act of Zfration
Abstract
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.
Document Details
- Document Type
- Technical Report
- Publication Date
- Sep 01, 2009
- Accession Number
- ADA512651
Entities
People
- Nan-Shan Chang
Organizations
- National Cheng Kung University