High-throughput discovery of Mycobacterium tuberculosis protein tyrosine phosphatase B (MptpB) inhibitors using click chemistry.
A approximately 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.
Departments of Biological Sciences, NUS MedChem Program of the Life Sciences Institute, National University of Singapore, Singapore 117543.
Lay Pheng
LP
Tan
Hao
H
Wu
Peng-Yu
PY
Yang
Karunakaran A
KA
Kalesh
Xiaohua
X
Zhang
Mingyu
M
Hu
Rajavel
R
Srinivasan
Shao Q
SQ
Yao
D001426:Bacterial Proteins / Q000037:antagonists & inhibitors*; D055808:Drug Discovery; D004791:Enzyme Inhibitors / Q000032:analysis* / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D057166:High-Throughput Screening Assays / Q000379:methods*; D015394:Molecular Structure; D017027:Protein Tyrosine Phosphatases / Q000037:antagonists & inhibitors*; D054852:Small Molecule Libraries; D013237:Stereoisomerism; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D004791:Enzyme Inhibitors; C414465:MptpA protein, Mycobacterium tuberculosis; D054852:Small Molecule Libraries; D017027:Protein Tyrosine Phosphatases