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Rapid assembly and in situ screening of bidentate inhibitors of protein tyrosine phosphatases
Rapid assembly and in situ screening of bidentate inhibitors of protein tyrosine phosphatases
- Source :
- Organic letters. 8(4)
- Publication Year :
- 2006
-
Abstract
- [reaction: see text] We have successfully designed and synthesized a small library of protein tyrosine phosphatase (PTP) inhibitors, in which the so-called "click chemistry" or Cu(I)-catalyzed 1,3-dipolar alkyne-azide coupling reaction was carried out for rapid assembly of 66 different bidentate compounds. Subsequent in situ enzymatic screening revealed a potential PTP1B inhibitor (IC(50) = 4.7 microM) which is 10-100 fold more potent than other PTPs.
- Subjects :
- chemistry.chemical_classification
In situ
Protein Tyrosine Phosphatase, Non-Receptor Type 1
Denticity
Binding Sites
Molecular Structure
Organic Chemistry
Protein tyrosine phosphatase
Isoxazoles
Triazoles
Biochemistry
Coupling reaction
Inhibitory Concentration 50
Enzyme
chemistry
Click chemistry
Combinatorial Chemistry Techniques
Physical and Theoretical Chemistry
Protein Tyrosine Phosphatases
IC50
Subjects
Details
- ISSN :
- 15237060
- Volume :
- 8
- Issue :
- 4
- Database :
- OpenAIRE
- Journal :
- Organic letters
- Accession number :
- edsair.doi.dedup.....20ef17f7cf6fc18b2c6d2f22d38eeac5