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J Proteome Res. 2002 Jan-Feb;1(1):35-40.

Design and synthesis of class-selective activity probes for protein tyrosine phosphatases.

Author information

1
Department of Chemistry, National Taiwan University, Taipei 106, Taiwan. lclo@ccms.ntu.edu.tw

Abstract

Two mechanism-based activity probes, adopting a cassette-like design, for protein tyrosine phosphatases (PTPs) were synthesized. Both probes carry a phosphate group that serves as the recognition head for the target PTPs but differ in their reporter groups; probe LCL-1 uses a dansyl fluorophore, while LCL-2 has a biotin reporter group. LCL-1 and LCL-2 are specifically activated by phosphatase, leading to its covalent labeling, as exemplified with PTP-1B. However, they show no activation with other classes of hydrolases, including trypsin and beta-galactosidase. LCL-1 and LCL-2 thus represent the first example of class-selective probes for phosphatases.

PMID:
12643524
[Indexed for MEDLINE]

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