Development of Tunable Activity Probes for Protein Tyrosine Phosphatase
Date Issued
2007
Date
2007
Author(s)
Huang, Yu-Yuan
DOI
zh-TW
Abstract
Protein tyrosine phosphatases (PTPs) played crucial role in physiology, participate in such work as cell growth, differentiation, and metabolism. Here we developed three activity probes for PTPs.
Hydrolysis of these activity probes by PTP appeared to be specific, rendering their selective labeling to PTP. When the P-OAr bond in our probes is cleaved by PTP. It quickly undergoes 1,4-elimination of the fluoride, hence resulting in the formation of the highly electrophilic quinone methide. The quinone methide could alkylate the nearby nucleophiles on the phosphatases.
A complete activity probe contains four structural units: (1) recognition head; (2) trapping device; (3) linker; (4) reporter group. We synthesized three regulable activity probes by tripeptide sequence.
Subjects
活性標示
水解酵素
PTP
activity probe
phosphatase
Type
thesis
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