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

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...

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Veröffentlicht in:Organic letters 2006-02, Vol.8 (4), p.713-716
Hauptverfasser: Srinivasan, Rajavel, Uttamchandani, Mahesh, Yao, Shao Q
Format: Artikel
Sprache:eng
Schlagworte:
Binding Sites - drug effects
Combinatorial Chemistry Techniques
Inhibitory Concentration 50
Isoxazoles - chemical synthesis
Isoxazoles - chemistry
Isoxazoles - pharmacology
Molecular Structure
Protein Tyrosine Phosphatase, Non-Receptor Type 1
Protein Tyrosine Phosphatases - antagonists & inhibitors
Triazoles - chemical synthesis
Triazoles - chemistry
Triazoles - pharmacology
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Zusammenfassung: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 (IC50 = 4.7 μM) which is 10−100 fold more potent than other PTPs.
ISSN:1523-7060
1523-7052
DOI:10.1021/ol052895w