Compounds > 1-2-3-4-tetrahydropyrimidine-2-thione

1-2-3-4-tetrahydropyrimidine-2-thione and Pseudomonas-Infections

1-2-3-4-tetrahydropyrimidine-2-thione has been researched along with Pseudomonas-Infections* in 1 studies

Other Studies

1 other study(ies) available for 1-2-3-4-tetrahydropyrimidine-2-thione and Pseudomonas-Infections

Article	Year
Synthesis and kinetic testing of tetrahydropyrimidine-2-thione and pyrrole derivatives as inhibitors of the metallo-β-lactamase from Klebsiella pneumonia and Pseudomonas aeruginosa. Chemical biology & drug design, 2012, Volume: 80, Issue:4 Metallo-β-lactamases (MBLs), produced by an increasing number of bacterial pathogens, facilitate the hydrolysis of many commonly used β-lactam antibiotics. There are no clinically useful antagonists against MBLs. Two sets of tetrahydropyrimidine-2-thione and pyrrole derivatives were synthesized and assayed for their inhibitory effects on the catalytic activity of the IMP-1 MBL from Pseudomonas aeruginosa and Klebsiella pneumoniae. Nine compounds tested (1a, 3b, 5c, 6b, 7a, 8a, 11c, 13a, and 16a) showed micromolar inhibition constants (K(i) values range from ∼20-80 μM). Compounds 1c, 2b, and 15a showed only weak inhibition. In silico docking was employed to investigate the binding mode of each enantiomer of the strongest inhibitor, 5c (K(i) = 19 ± 9 μM), as well as 7a (K(i) =21 ± 10 μM), the strongest inhibitor of the pyrrole series, in the active site of IMP-1. Topics: Anti-Bacterial Agents; beta-Lactamase Inhibitors; beta-Lactamases; Humans; Klebsiella Infections; Klebsiella pneumoniae; Molecular Docking Simulation; Pseudomonas aeruginosa; Pseudomonas Infections; Pyrimidines; Pyrroles; Structure-Activity Relationship	2012

Article

Year

Synthesis and kinetic testing of tetrahydropyrimidine-2-thione and pyrrole derivatives as inhibitors of the metallo-β-lactamase from Klebsiella pneumonia and Pseudomonas aeruginosa.

Chemical biology & drug design, 2012, Volume: 80, Issue:4

Metallo-β-lactamases (MBLs), produced by an increasing number of bacterial pathogens, facilitate the hydrolysis of many commonly used β-lactam antibiotics. There are no clinically useful antagonists against MBLs. Two sets of tetrahydropyrimidine-2-thione and pyrrole derivatives were synthesized and assayed for their inhibitory effects on the catalytic activity of the IMP-1 MBL from Pseudomonas aeruginosa and Klebsiella pneumoniae. Nine compounds tested (1a, 3b, 5c, 6b, 7a, 8a, 11c, 13a, and 16a) showed micromolar inhibition constants (K(i) values range from ∼20-80 μM). Compounds 1c, 2b, and 15a showed only weak inhibition. In silico docking was employed to investigate the binding mode of each enantiomer of the strongest inhibitor, 5c (K(i) = 19 ± 9 μM), as well as 7a (K(i) =21 ± 10 μM), the strongest inhibitor of the pyrrole series, in the active site of IMP-1.

Topics: Anti-Bacterial Agents; beta-Lactamase Inhibitors; beta-Lactamases; Humans; Klebsiella Infections; Klebsiella pneumoniae; Molecular Docking Simulation; Pseudomonas aeruginosa; Pseudomonas Infections; Pyrimidines; Pyrroles; Structure-Activity Relationship

2012