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A G-Quadruplex Aptamer Inhibits the Phosphatase Activity of Oncogenic Protein Shp2 in vitro

✍ Scribed by Jia Hu; Jie Wu; Cong Li; Ling Zhu; Dr. Wei Yun Zhang; Guiping Kong; Prof. Zhongxian Lu; Prof. Chaoyong James Yang

Publisher
John Wiley and Sons
Year
2011
Tongue
English
Weight
653 KB
Volume
12
Category
Article
ISSN
1439-4227

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✦ Synopsis

Abstract

Shp2 is a member of the protein tyrosine phosphatase (PTP) family, which regulates a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. Using a recombinant Shp2‐GST protein as the target and GST as a counter target, we have identified two classes of single‐stranded DNA aptamers that selectively bind to Shp2 with a K~d~ in the nanomolar range. Structural studies of the most abundant sequence in the enriched library, HJ24, revealed a parallel G‐quadruplex as the core binding domain. Furthermore, this aptamer was found to be an effective inhibitor of Shp2 phosphatase, an effect which was readily reversed by using the cDNA of HJ24. In view of these characteristics, this aptamer has the potential to be used for further development of Shp2 assays and therapeutics for the treatment of Shp2‐dependent cancers and other diseases.

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