|
Antimicrobial activity against Staphylococcus aureus after 24 hrs by broth microdilution method
|
Staphylococcus aureus
|
1.82
ug.mL-1
|
|
Journal : Eur. J. Med. Chem.
Title : Synthesis, characterization and in vitro antibacterial activity of new steroidal 5-en-3-oxazolo and thiazoloquinoxaline.
Year : 2008
Volume : 43
Issue : 9
First Page : 2040
Last Page : 2044
Authors : Khan SA.
Abstract : Steriodal heterocyclic systems namely cholest-5-en-3-oxazolo and thiazoloquinoxaline have been synthesized via the reaction of cholest-5-en-3-one semicarbazone/thiosemicarbazone with 2,3-dichloroquinoxaline at 80 degrees C in high yield. Cholest-5-en-3-one semicarbazone is obtained by the condensation of cholest-5-en-3-one with semicarbazide in the presence of AcONa in ethanol and cholest-5-en-one thiosemicarbazone is obtained by the condensation of cholest-5-en-3-one with thiosemicarbazide in ethanol in the presence of a few drops of HCl. The structures of these compounds were evident by elemental analysis, IR, 1H NMR and FAB mass spectral analysis. These synthesized compounds were investigated for antibacterial activity first by the disk-diffusion assay against two Gram-positive and two Gram-negative bacteria and then the minimum inhibitory concentration (MIC) of these compounds were determined and the results were compared with the standard drug Amoxicillin. The results showed that these compounds oxazolo/thiazoloquinoxaline are better antibacterial agents as compared to the standard drug Amoxicillin.
|
Antimicrobial activity against Streptococcus pyogenes after 24 hrs by broth microdilution method
|
Streptococcus pyogenes
|
1.8
ug.mL-1
|
|
Journal : Eur. J. Med. Chem.
Title : Synthesis, characterization and in vitro antibacterial activity of new steroidal 5-en-3-oxazolo and thiazoloquinoxaline.
Year : 2008
Volume : 43
Issue : 9
First Page : 2040
Last Page : 2044
Authors : Khan SA.
Abstract : Steriodal heterocyclic systems namely cholest-5-en-3-oxazolo and thiazoloquinoxaline have been synthesized via the reaction of cholest-5-en-3-one semicarbazone/thiosemicarbazone with 2,3-dichloroquinoxaline at 80 degrees C in high yield. Cholest-5-en-3-one semicarbazone is obtained by the condensation of cholest-5-en-3-one with semicarbazide in the presence of AcONa in ethanol and cholest-5-en-one thiosemicarbazone is obtained by the condensation of cholest-5-en-3-one with thiosemicarbazide in ethanol in the presence of a few drops of HCl. The structures of these compounds were evident by elemental analysis, IR, 1H NMR and FAB mass spectral analysis. These synthesized compounds were investigated for antibacterial activity first by the disk-diffusion assay against two Gram-positive and two Gram-negative bacteria and then the minimum inhibitory concentration (MIC) of these compounds were determined and the results were compared with the standard drug Amoxicillin. The results showed that these compounds oxazolo/thiazoloquinoxaline are better antibacterial agents as compared to the standard drug Amoxicillin.
|
Antimicrobial activity against Salmonella Typhimurium after 24 hrs by broth microdilution method
|
Salmonella enterica subsp. enterica serovar Typhimurium
|
1.85
ug.mL-1
|
|
Journal : Eur. J. Med. Chem.
Title : Synthesis, characterization and in vitro antibacterial activity of new steroidal 5-en-3-oxazolo and thiazoloquinoxaline.
Year : 2008
Volume : 43
Issue : 9
First Page : 2040
Last Page : 2044
Authors : Khan SA.
Abstract : Steriodal heterocyclic systems namely cholest-5-en-3-oxazolo and thiazoloquinoxaline have been synthesized via the reaction of cholest-5-en-3-one semicarbazone/thiosemicarbazone with 2,3-dichloroquinoxaline at 80 degrees C in high yield. Cholest-5-en-3-one semicarbazone is obtained by the condensation of cholest-5-en-3-one with semicarbazide in the presence of AcONa in ethanol and cholest-5-en-one thiosemicarbazone is obtained by the condensation of cholest-5-en-3-one with thiosemicarbazide in ethanol in the presence of a few drops of HCl. The structures of these compounds were evident by elemental analysis, IR, 1H NMR and FAB mass spectral analysis. These synthesized compounds were investigated for antibacterial activity first by the disk-diffusion assay against two Gram-positive and two Gram-negative bacteria and then the minimum inhibitory concentration (MIC) of these compounds were determined and the results were compared with the standard drug Amoxicillin. The results showed that these compounds oxazolo/thiazoloquinoxaline are better antibacterial agents as compared to the standard drug Amoxicillin.
|
Antimicrobial activity against Escherichia coli after 24 hrs by broth microdilution method
|
Escherichia coli
|
1.9
ug.mL-1
|
|
Journal : Eur. J. Med. Chem.
Title : Synthesis, characterization and in vitro antibacterial activity of new steroidal 5-en-3-oxazolo and thiazoloquinoxaline.
Year : 2008
Volume : 43
Issue : 9
First Page : 2040
Last Page : 2044
Authors : Khan SA.
Abstract : Steriodal heterocyclic systems namely cholest-5-en-3-oxazolo and thiazoloquinoxaline have been synthesized via the reaction of cholest-5-en-3-one semicarbazone/thiosemicarbazone with 2,3-dichloroquinoxaline at 80 degrees C in high yield. Cholest-5-en-3-one semicarbazone is obtained by the condensation of cholest-5-en-3-one with semicarbazide in the presence of AcONa in ethanol and cholest-5-en-one thiosemicarbazone is obtained by the condensation of cholest-5-en-3-one with thiosemicarbazide in ethanol in the presence of a few drops of HCl. The structures of these compounds were evident by elemental analysis, IR, 1H NMR and FAB mass spectral analysis. These synthesized compounds were investigated for antibacterial activity first by the disk-diffusion assay against two Gram-positive and two Gram-negative bacteria and then the minimum inhibitory concentration (MIC) of these compounds were determined and the results were compared with the standard drug Amoxicillin. The results showed that these compounds oxazolo/thiazoloquinoxaline are better antibacterial agents as compared to the standard drug Amoxicillin.
|
Inhibition of Helicobacter pylori invasion into human AGS cells at 2.5 uM after 6 hrs
|
Helicobacter pylori
|
90.0
%
|
|
Journal : Bioorg. Med. Chem. Lett.
Title : Identification of 3',4',5'-trimethoxychalcone analogues as potent inhibitors of Helicobacter pylori-induced inflammation in human gastric epithelial cells.
Year : 2010
Volume : 20
Issue : 18
First Page : 5462
Last Page : 5465
Authors : Lai CH, Rao YK, Fang SH, Sing YT, Tzeng YM.
Abstract : Efforts to identify potent small molecule inhibitors of Helicobacter pylori led to the evaluation of 23 3',4',5'-trimethoxychalcone analogues. Some of the compounds displayed potent antibacterial activity against H. pylori. Three most active and selective compounds 1, 7, and 13 also showed the bactericide activity against the reference as well as multidrug-resistant strains of H. pylori. Additionally, the aforementioned three compounds potentially inhibited the H. pylori adhesion and invasion to human gastric epithelial (AGS) cells. Furthermore, these selective compounds inhibited the H. pylori-induced gastric inflammation by reduced inflammatory mediator's nuclear factor kappa B activation, and the secretion of interleukin-8.
|
Inhibition of Helicobacter pylori-induced inflammation in human AGS cells assessed as reduction of IL-8 production at 10 uM by ELISA
|
Helicobacter pylori
|
81.9
%
|
|
Journal : Bioorg. Med. Chem. Lett.
Title : Identification of 3',4',5'-trimethoxychalcone analogues as potent inhibitors of Helicobacter pylori-induced inflammation in human gastric epithelial cells.
Year : 2010
Volume : 20
Issue : 18
First Page : 5462
Last Page : 5465
Authors : Lai CH, Rao YK, Fang SH, Sing YT, Tzeng YM.
Abstract : Efforts to identify potent small molecule inhibitors of Helicobacter pylori led to the evaluation of 23 3',4',5'-trimethoxychalcone analogues. Some of the compounds displayed potent antibacterial activity against H. pylori. Three most active and selective compounds 1, 7, and 13 also showed the bactericide activity against the reference as well as multidrug-resistant strains of H. pylori. Additionally, the aforementioned three compounds potentially inhibited the H. pylori adhesion and invasion to human gastric epithelial (AGS) cells. Furthermore, these selective compounds inhibited the H. pylori-induced gastric inflammation by reduced inflammatory mediator's nuclear factor kappa B activation, and the secretion of interleukin-8.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 24 PBP1A
|
Streptococcus pneumoniae
|
0.004
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3413 PBP1A
|
Streptococcus pneumoniae
|
0.124
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 2527 PBP1A
|
Streptococcus pneumoniae
|
0.049
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3676 PBP1A
|
Streptococcus pneumoniae
|
0.422
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3243 PBP1A
|
Streptococcus pneumoniae
|
0.059
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3665 PBP1A
|
Streptococcus pneumoniae
|
0.067
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3009 PBP1A
|
Streptococcus pneumoniae
|
0.09
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 1076 PBP1A
|
Streptococcus pneumoniae
|
0.044
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 1077 PBP1A
|
Streptococcus pneumoniae
|
0.017
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 24 PBP1B
|
Streptococcus pneumoniae
|
1.103
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3413 PBP1B
|
Streptococcus pneumoniae
|
0.035
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 2527 PBP1B
|
Streptococcus pneumoniae
|
0.029
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3676 PBP1B
|
Streptococcus pneumoniae
|
0.116
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3243 PBP1B
|
Streptococcus pneumoniae
|
0.165
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3665 PBP1B
|
Streptococcus pneumoniae
|
0.079
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3009 PBP1B
|
Streptococcus pneumoniae
|
0.059
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 1076 PBP1B
|
Streptococcus pneumoniae
|
0.068
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 1077 PBP1B
|
Streptococcus pneumoniae
|
0.006
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 24 PBP2X
|
Streptococcus pneumoniae
|
0.117
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3413 PBP2X
|
Streptococcus pneumoniae
|
0.062
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 2527 PBP2X
|
Streptococcus pneumoniae
|
0.004
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3676 PBP2X
|
Streptococcus pneumoniae
|
0.043
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3243 PBP2X
|
Streptococcus pneumoniae
|
0.018
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3665 PBP2X
|
Streptococcus pneumoniae
|
0.094
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3009 PBP2X
|
Streptococcus pneumoniae
|
0.008
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 1076 PBP2X
|
Streptococcus pneumoniae
|
0.037
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 1077 PBP2X
|
Streptococcus pneumoniae
|
0.022
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 24 PBP2A
|
Streptococcus pneumoniae
|
0.077
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3413 PBP2A
|
Streptococcus pneumoniae
|
0.034
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 2527 PBP2A
|
Streptococcus pneumoniae
|
0.051
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3676 PBP2A
|
Streptococcus pneumoniae
|
0.066
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3665 PBP2A
|
Streptococcus pneumoniae
|
0.05
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3009 PBP2A
|
Streptococcus pneumoniae
|
0.08
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 1076 PBP2A
|
Streptococcus pneumoniae
|
0.08
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 24 PBP2B
|
Streptococcus pneumoniae
|
0.176
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3413 PBP2B
|
Streptococcus pneumoniae
|
0.165
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 2527 PBP2B
|
Streptococcus pneumoniae
|
0.033
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3676 PBP2B
|
Streptococcus pneumoniae
|
0.144
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3243 PBP2B
|
Streptococcus pneumoniae
|
0.029
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3665 PBP2B
|
Streptococcus pneumoniae
|
0.22
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3009 PBP2B
|
Streptococcus pneumoniae
|
0.05
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 1076 PBP2B
|
Streptococcus pneumoniae
|
0.055
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 1077 PBP2B
|
Streptococcus pneumoniae
|
0.03
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 24 PBP3
|
Streptococcus pneumoniae
|
0.049
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3413 PBP3
|
Streptococcus pneumoniae
|
0.029
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 2527 PBP3
|
Streptococcus pneumoniae
|
0.022
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3676 PBP3
|
Streptococcus pneumoniae
|
0.019
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3243 PBP3
|
Streptococcus pneumoniae
|
0.006
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3665 PBP3
|
Streptococcus pneumoniae
|
0.019
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3009 PBP3
|
Streptococcus pneumoniae
|
0.047
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 1076 PBP3
|
Streptococcus pneumoniae
|
0.051
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 1077 PBP3
|
Streptococcus pneumoniae
|
0.022
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Antibacterial activity against Staphylococcus aureus
|
Staphylococcus aureus
|
2.84
ug.mL-1
|
|
Journal : Bioorg. Med. Chem. Lett.
Title : Microwave-assisted synthesis and in vitro antibacterial activity of novel steroidal thiosemicarbazone derivatives.
Year : 2012
Volume : 22
Issue : 24
First Page : 7730
Last Page : 7734
Authors : Zhao Z, Shi Z, Liu M, Liu X.
Abstract : Herein, we reported the synthesis of 16 novel steroidal thiosemicarbazone derivatives via the condensation of steroidal ketones and substituted thiosemicarbazides under solvent-free conditions using microwave irradiation. The yields obtained are in the range of 84-96% using microwave method and 46-62% using conventional method. All the synthesized compounds (7a-p) have been characterized by (1)H NMR, ESI-MS, IR and elemental analyses. All the series compounds (7a-p) were evaluated for their antibacterial activity against and the results were compared with the standard drug Amoxicillin. Some of the compounds from the series like 7c, 7o and 7p were equipotent with Amoxicillin against Pseudomonas aeruginosa. Also compound 7h was better than Amoxicillin against Staphylococcus aureus and Bacillus subtilis.
|
Inhibition of sodium fluorescein uptake in OATP1B1-transfected CHO cells at an equimolar substrate-inhibitor concentration of 10 uM
|
Cricetulus griseus
|
75.16
%
|
|
Journal : Mol. Pharmacol.
Title : Structure-based identification of OATP1B1/3 inhibitors.
Year : 2013
Volume : 83
Issue : 6
First Page : 1257
Last Page : 1267
Authors : De Bruyn T, van Westen GJ, Ijzerman AP, Stieger B, de Witte P, Augustijns PF, Annaert PP.
Abstract : Several recent studies show that inhibition of the hepatic transport proteins organic anion-transporting polypeptide 1B1 (OATP1B1) and 1B3 (OATP1B3) can result in clinically relevant drug-drug interactions (DDI). To avoid late-stage development drug failures due to OATP1B-mediated DDI, predictive in vitro and in silico methods should be implemented at an early stage of the drug candidate evaluation process. In the present study, we first developed a high-throughput in vitro transporter inhibition assay for the OATP1B subfamily. A total of 2000 compounds were tested as potential modulators of the uptake of the OATP1B substrate sodium fluorescein, in OATP1B1- or 1B3-transfected Chinese hamster ovary cells. At an equimolar substrate-inhibitor concentration of 10 µM, 212 and 139 molecules were identified as OATP1B1 and OATP1B3 inhibitors, respectively (minimum 50% inhibition). For 69 compounds, previously not identified as OATP1B inhibitors, concentration-dependent inhibition was also determined, yielding Ki values ranging from 0.06 to 6.5 µM. Based on these in vitro data, we subsequently developed a proteochemometrics-based in silico model, which predicted OATP1B inhibitors in the test group (20% of the dataset) with high specificity (86%) and sensitivity (78%). Moreover, several physicochemical compound properties and substructures related to OATP1B1/1B3 inhibition or inactivity were identified. Finally, model performance was prospectively verified with a set of 54 compounds not included in the original dataset. This validation indicated that 80 and 74% of the compounds were correctly classified for OATP1B1 and OATP1B3 inhibition, respectively.
|
Inhibition of sodium fluorescein uptake in OATP1B3-transfected CHO cells at an equimolar substrate-inhibitor concentration of 10 uM
|
Cricetulus griseus
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87.94
%
|
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Journal : Mol. Pharmacol.
Title : Structure-based identification of OATP1B1/3 inhibitors.
Year : 2013
Volume : 83
Issue : 6
First Page : 1257
Last Page : 1267
Authors : De Bruyn T, van Westen GJ, Ijzerman AP, Stieger B, de Witte P, Augustijns PF, Annaert PP.
Abstract : Several recent studies show that inhibition of the hepatic transport proteins organic anion-transporting polypeptide 1B1 (OATP1B1) and 1B3 (OATP1B3) can result in clinically relevant drug-drug interactions (DDI). To avoid late-stage development drug failures due to OATP1B-mediated DDI, predictive in vitro and in silico methods should be implemented at an early stage of the drug candidate evaluation process. In the present study, we first developed a high-throughput in vitro transporter inhibition assay for the OATP1B subfamily. A total of 2000 compounds were tested as potential modulators of the uptake of the OATP1B substrate sodium fluorescein, in OATP1B1- or 1B3-transfected Chinese hamster ovary cells. At an equimolar substrate-inhibitor concentration of 10 µM, 212 and 139 molecules were identified as OATP1B1 and OATP1B3 inhibitors, respectively (minimum 50% inhibition). For 69 compounds, previously not identified as OATP1B inhibitors, concentration-dependent inhibition was also determined, yielding Ki values ranging from 0.06 to 6.5 µM. Based on these in vitro data, we subsequently developed a proteochemometrics-based in silico model, which predicted OATP1B inhibitors in the test group (20% of the dataset) with high specificity (86%) and sensitivity (78%). Moreover, several physicochemical compound properties and substructures related to OATP1B1/1B3 inhibition or inactivity were identified. Finally, model performance was prospectively verified with a set of 54 compounds not included in the original dataset. This validation indicated that 80 and 74% of the compounds were correctly classified for OATP1B1 and OATP1B3 inhibition, respectively.
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Antibacterial activity against Staphylococcus aureus MRSA ATCC 43300 (CO-ADD:GP_020); MIC in CAMBH media, using NBS plates, by OD(600)
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Staphylococcus aureus subsp. aureus
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15.09
%
|
|
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Antibacterial activity against Escherichia coli ATCC 25922 (CO-ADD:GN_001); MIC in CAMBH media using NBS plates, by OD(600)
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Escherichia coli
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7.14
%
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|
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Antibacterial activity against Klebsiella pneumoniae MDR ATCC 70063 (CO-ADD:GN_003); MIC in CAMBH media using NBS plates, by OD(600)
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Klebsiella pneumoniae
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10.29
%
|
|
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Antibacterial activity against Pseudomonas aeruginosa ATCC 27853 (CO-ADD:GN_042); MIC in CAMBH media using NBS plates, by OD(600)
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Pseudomonas aeruginosa
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10.8
%
|
|
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Antibacterial activity against Acinetobacter baumannii ATCC 19606 (CO-ADD:GN_034); MIC in CAMBH media using NBS plates, by OD600
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Acinetobacter baumannii
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22.8
%
|
|
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Antifungal activity against Candida albicans ATCC 90028 (CO-ADD:FG_001); MIC in YNB media using NBS plates, by OD630
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Candida albicans
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9.25
%
|
|
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Antifungal activity against Cryptococcus neoformans H99 ATCC 208821 (CO-ADD:FG_002); MIC in YNB media using NBS plates, by Resazurin OD(600-570)
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Cryptococcus neoformans
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-2.09
%
|
|
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Antiviral activity determined as inhibition of SARS-CoV-2 induced cytotoxicity of Caco-2 cells at 10 uM after 48 hours by high content imaging
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Homo sapiens
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1.48
%
|
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Title : Identification of inhibitors of SARS-CoV-2 in-vitro cellular toxicity in human (Caco-2) cells using a large scale drug repurposing collection
Year : 2020
Authors : Bernhard Ellinger, Denisa Bojkova, Andrea Zaliani, Jindrich Cinatl, Carsten Claussen, Sandra Westhaus, Jeanette Reinshagen, Maria Kuzikov, Markus Wolf, Gerd Geisslinger, Philip Gribbon, Sandra Ciesek
Abstract : To identify possible candidates for progression towards clinical studies against SARS-CoV-2, we screened a well-defined collection of 5632 compounds including 3488 compounds which have undergone clinical investigations (marketed drugs, phases 1 -3, and withdrawn) across 600 indications. Compounds were screened for their inhibition of viral induced cytotoxicity using the human epithelial colorectal adenocarcinoma cell line Caco-2 and a SARS-CoV-2 isolate. The primary screen of 5632 compounds gave 271 hits. A total of 64 compounds with IC50 <20 µM were identified, including 19 compounds with IC50 < 1 µM. Of this confirmed hit population, 90% have not yet been previously reported as active against SARS-CoV-2 in-vitro cell assays. Some 37 of the actives are launched drugs, 19 are in phases 1-3 and 10 pre-clinical. Several inhibitors were associated with modulation of host pathways including kinase signaling P53 activation, ubiquitin pathways and PDE activity modulation, with long chain acyl transferases were effective viral inhibitors.
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SARS-CoV-2 3CL-Pro protease inhibition percentage at 20µM by FRET kind of response from peptide substrate
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Severe acute respiratory syndrome coronavirus 2
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11.63
%
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Title : Identification of inhibitors of SARS-Cov2 M-Pro enzymatic activity using a small molecule repurposing screen
Year : 2020
Authors : Maria Kuzikov, Elisa Costanzi, Jeanette Reinshagen, Francesca Esposito, Laura Vangeel, Markus Wolf, Bernhard Ellinger, Carsten Claussen, Gerd Geisslinger, Angela Corona, Daniela Iaconis, Carmine Talarico, Candida Manelfi, Rolando Cannalire, Giulia Rossetti, Jonas Gossen, Simone Albani, Francesco Musiani, Katja Herzog, Yang Ye, Barbara Giabbai, Nicola Demitri, Dirk Jochmans, Steven De Jonghe, Jasper Rymenants, Vincenzo Summa, Enzo Tramontano, Andrea R. Beccari, Pieter Leyssen, Paola Storici, Johan Neyts, Philip Gribbon, and Andrea Zaliani
Abstract : Compound repurposing is an important strategy being pursued in the identification of effective treatment against the SARS-CoV-2 infection and COVID-19 disease. In this regard, SARS-CoV-2 main protease (M-Pro), also termed 3CL-Pro, is an attractive drug target as it plays a central role in viral replication by processing the viral polyprotein into 11 non-structural proteins. We report the results of a screening campaign involving ca 8.7 K compounds containing marketed drugs, clinical and preclinical candidates, and chemicals regarded as safe in humans. We confirmed previously reported inhibitors of 3CL-Pro, but we have also identified 68 compounds with IC50 lower than 1 uM and 127 compounds with IC50 lower than 5 uM. Profiling showed 67% of confirmed hits were selective (> 5 fold) against other Cys- and Ser- proteases (Chymotrypsin and Cathepsin-L) and MERS 3CL-Pro. Selected compounds were also analysed in their binding characteristics.
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Antiviral activity determined as inhibition of SARS-CoV-2 induced cytotoxicity of VERO-6 cells at 10 uM after 48 hours exposure to 0.01 MOI SARS CoV-2 virus by high content imaging
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Chlorocebus sabaeus
|
-0.02
%
|
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Antiviral activity determined as inhibition of SARS-CoV-2 induced cytotoxicity of VERO-6 cells at 10 uM after 48 hours exposure to 0.01 MOI SARS CoV-2 virus by high content imaging
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Chlorocebus sabaeus
|
-0.02
%
|
|
Title : Cytopathic SARS-Cov2 screening on VERO-E6 cells in a large repurposing effort
Year : 2020
Authors : Andrea Zaliani, Laura Vangeel, Jeanette Reinshagen, Daniela Iaconis, Maria Kuzikov, Oliver Keminer, Markus Wolf, Bernhard Ellinger, Francesca Esposito, Angela Corona, Enzo Tramontano, Candida Manelfi, Katja Herzog, Dirk Jochmans, Steven De Jonghe, Winston Chiu, Thibault Francken, Joost Schepers, Caroline Collard, Kayvan Abbasi, Carsten Claussen , Vincenzo Summa, Andrea R. Beccari, Johan Neyts, Philip Gribbon and Pieter Leyssen
Abstract : Worldwide, there are intensive efforts to identify repurposed drugs as potential therapies against SARS-CoV-2 infection and the associated COVID-19 disease. To date, the anti-inflammatory drug dexamethasone and (to a lesser extent) the RNA-polymerase inhibitor remdesivir have been shown to be effective in reducing mortality and patient time to recovery, respectively, in patients. Here, we report the results of a phenotypic screening campaign within an EU-funded project (H2020-EXSCALATE4COV) aimed at extending the repertoire of anti-COVID therapeutics through repurposing of available compounds and highlighting compounds with new mechanisms of action against viral infection. We screened 8702 molecules from different repurposing libraries, to reveal 110 compounds with an anti-cytopathic IC50 < 20 µM. From this group, 18 with a safety index greater than 2 are also marketed drugs, making them suitable for further study as potential therapies against COVID-19. Our result supports the idea that a systematic approach to repurposing is a valid strategy to accelerate the necessary drug discovery process.
