Design and Synthesis of an Activity Probe for Protein Tyrosine Phosphatases
Resource
Journal of the Chinese Chemical Society 46 (5): 715-718
Journal
Journal of the Chinese Chemical Society
Journal Volume
46
Journal Issue
5
Pages
715-718
Date Issued
1999
Date
1999
Author(s)
Abstract
Abstract Protein tyrosine phosphatases (PTPases) are an important class of enzymes involved in the regulation of many cellular events. Here we describe the design and synthesis of an activity probe 2 targeting these PTPases. This mechanism‐based activity probe adopts a cassette‐like design; a phosphate group serves as the recognition head and a fluorescent diethylaminocoumarin derivative acts as the reporter group. Compound 3 was phosphorylated with diallyl phosphorochloridate and then fluorinated with DAST to give versatile intermediate 5. The Boc protective group of compound 5 was removed by TEA to make available the amino group where a diethylaminocoumarin chromophore was later attached. Final deprotection of the allyl group from the phosphate head gives our complete activity probe 2. It will be used in the labeling study of PTPases from various sources.
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Type
journal article
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