Design and Synthesis of Class-Selective Activity Probes for Protein Tyrosine Phosphatases | Zendy

LeeChiang Lo | Zendy; Te-Ling Pang | Zendy; ChiHsien Kuo | Zendy; YingLing Chiang | Zendy; HsinYi Wang | Zendy; JingJer Lin | Zendy

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Design and Synthesis of Class-Selective Activity Probes for Protein Tyrosine Phosphatases

Author(s) -

LeeChiang Lo,

Te-Ling Pang,

ChiHsien Kuo,

YingLing Chiang,

HsinYi Wang,

JingJer Lin

Publication year - 2002

Publication title -

journal of proteome research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.644

H-Index - 161

eISSN - 1535-3907

pISSN - 1535-3893

DOI - 10.1021/pr015506a

Subject(s) - protein tyrosine phosphatase , phosphatase , biochemistry , chemistry , tyrosine , fluorophore , biotin , proteomics , enzyme , biology , fluorescence , physics , quantum mechanics , gene

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.

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