High-Throughput Discovery of Mycobacterium tuberculosis Protein Tyrosine Phosphatase B (MptpB) Inhibitors Using Click Chemistry

A ∼3500-member library of bidentate inhibitors against protein tyrosine phosphatases (PTPs) was rapidly assembled using click chemistry. Subsequent high-throughput screening had led to the discovery of highly potent (K i as low as 150 nM) and selective MptpB inhibitors, some of which represent the m...

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Veröffentlicht in:	Organic letters 2009-11, Vol.11 (22), p.5102-5105
Hauptverfasser:	Tan, Lay Pheng, Wu, Hao, Yang, Peng-Yu, Kalesh, Karunakaran A, Zhang, Xiaohua, Hu, Mingyu, Srinivasan, Rajavel, Yao, Shao Q
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacterial Proteins - antagonists & inhibitors Drug Discovery Enzyme Inhibitors - analysis Enzyme Inhibitors - chemical synthesis Enzyme Inhibitors - chemistry Enzyme Inhibitors - pharmacology High-Throughput Screening Assays - methods Molecular Structure Protein Tyrosine Phosphatases - antagonists & inhibitors Small Molecule Libraries Stereoisomerism Structure-Activity Relationship
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Beschreibung
Zusammenfassung:	A ∼3500-member library of bidentate inhibitors against protein tyrosine phosphatases (PTPs) was rapidly assembled using click chemistry. Subsequent high-throughput screening had led to the discovery of highly potent (K i as low as 150 nM) and selective MptpB inhibitors, some of which represent the most potent MptpB inhibitors developed to date.
ISSN:	1523-7060 1523-7052
DOI:	10.1021/ol9023419