The Experts below are selected from a list of 105 Experts worldwide ranked by ideXlab platform
Shahriar Mobashery - One of the best experts on this subject based on the ideXlab platform.
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a mechanism based inhibitor targeting the dd transpeptidase activity of bacterial penicillin binding proteins
Journal of the American Chemical Society, 2003Co-Authors: Dusan Hesek, Maxim Suvorov, Sergei B Vakulenko, Shahriar MobasheryAbstract:Penicillin-binding proteins (PBPs) are responsible for the final stages of bacterial cell wall assembly. These enzymes are targets of β-lactam antibiotics. Two of the PBP activities include dd-transpeptidase and dd-carboxypeptidase activities, which carry out the cross-linking of the cell wall and trimming of the peptidoglycan, the major constituent of the cell wall, by an amino acid, respectively. The activity of the latter enzyme moderates the degree of cross-linking of the cell wall, which is carried out by the former. Both these enzymes go through an acyl-enzyme species in the course of their catalytic events. Compound 6, a Cephalosporin Derivative incorporated with structural features of the peptidoglycan was conceived as an inhibitor specific for dd-transpeptidases. On acylation of the active sites of dd-transpeptidases, the molecule would organize itself in the two active site subsites such that it mimics the two sequestered strands of the bacterial peptidoglycan en route to their cross-linking. He...
Elmar Dr Schrinner - One of the best experts on this subject based on the ideXlab platform.
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Antibacterial activities in vitro and in vivo and pharmacokinetics of cefquinome (HR 111V), a new broad-spectrum Cephalosporin.
Antimicrobial agents and chemotherapy, 1991Co-Authors: M. Limbert, Dieter Isert, N. Klesel, Astrid Markus, K Seeger, G. Seibert, Elmar Dr SchrinnerAbstract:Cefquinome is a new injectable aminothiazolyl Cephalosporin Derivative. It is stable against chromosomally and plasmid-encoded beta-lactamases and has a broad antibacterial spectrum. Staphylococcus aureus, streptococci, Pseudomonas aeruginosa, and members of the family Enterobacteriaceae (Escherichia coli, Salmonella spp., Klebsiella spp., Enterobacter spp., Citrobacter spp., and Serratia marcescens) are inhibited at low concentrations. Cefquinome is also active against many strains of methicillin-resistant staphylococci and enterococci. Its in vitro activity against gram-negative anaerobes is very limited. The high in vitro activity of cefquinome is reflected by its high in vivo efficacy against experimental septicemia due to different gram-positive and gram-negative bacteria. We studied the pharmacokinetic properties of cefquinome in mice, dogs, pigs, and calves. After single parenteral administrations, cefquinome displayed high peak levels, declining with half-lives of about 0.5, 0.9, 1.2, and 1.3 h, respectively. The areas under the concentration-time curve determined for dogs and mice showed linear correlations to the given doses. In dogs the urinary recovery was more than 70% within 24 h of dosing.
Dusan Hesek - One of the best experts on this subject based on the ideXlab platform.
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a mechanism based inhibitor targeting the dd transpeptidase activity of bacterial penicillin binding proteins
Journal of the American Chemical Society, 2003Co-Authors: Dusan Hesek, Maxim Suvorov, Sergei B Vakulenko, Shahriar MobasheryAbstract:Penicillin-binding proteins (PBPs) are responsible for the final stages of bacterial cell wall assembly. These enzymes are targets of β-lactam antibiotics. Two of the PBP activities include dd-transpeptidase and dd-carboxypeptidase activities, which carry out the cross-linking of the cell wall and trimming of the peptidoglycan, the major constituent of the cell wall, by an amino acid, respectively. The activity of the latter enzyme moderates the degree of cross-linking of the cell wall, which is carried out by the former. Both these enzymes go through an acyl-enzyme species in the course of their catalytic events. Compound 6, a Cephalosporin Derivative incorporated with structural features of the peptidoglycan was conceived as an inhibitor specific for dd-transpeptidases. On acylation of the active sites of dd-transpeptidases, the molecule would organize itself in the two active site subsites such that it mimics the two sequestered strands of the bacterial peptidoglycan en route to their cross-linking. He...
M. Limbert - One of the best experts on this subject based on the ideXlab platform.
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Antibacterial activities in vitro and in vivo and pharmacokinetics of cefquinome (HR 111V), a new broad-spectrum Cephalosporin.
Antimicrobial agents and chemotherapy, 1991Co-Authors: M. Limbert, Dieter Isert, N. Klesel, Astrid Markus, K Seeger, G. Seibert, Elmar Dr SchrinnerAbstract:Cefquinome is a new injectable aminothiazolyl Cephalosporin Derivative. It is stable against chromosomally and plasmid-encoded beta-lactamases and has a broad antibacterial spectrum. Staphylococcus aureus, streptococci, Pseudomonas aeruginosa, and members of the family Enterobacteriaceae (Escherichia coli, Salmonella spp., Klebsiella spp., Enterobacter spp., Citrobacter spp., and Serratia marcescens) are inhibited at low concentrations. Cefquinome is also active against many strains of methicillin-resistant staphylococci and enterococci. Its in vitro activity against gram-negative anaerobes is very limited. The high in vitro activity of cefquinome is reflected by its high in vivo efficacy against experimental septicemia due to different gram-positive and gram-negative bacteria. We studied the pharmacokinetic properties of cefquinome in mice, dogs, pigs, and calves. After single parenteral administrations, cefquinome displayed high peak levels, declining with half-lives of about 0.5, 0.9, 1.2, and 1.3 h, respectively. The areas under the concentration-time curve determined for dogs and mice showed linear correlations to the given doses. In dogs the urinary recovery was more than 70% within 24 h of dosing.
Maxim Suvorov - One of the best experts on this subject based on the ideXlab platform.
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a mechanism based inhibitor targeting the dd transpeptidase activity of bacterial penicillin binding proteins
Journal of the American Chemical Society, 2003Co-Authors: Dusan Hesek, Maxim Suvorov, Sergei B Vakulenko, Shahriar MobasheryAbstract:Penicillin-binding proteins (PBPs) are responsible for the final stages of bacterial cell wall assembly. These enzymes are targets of β-lactam antibiotics. Two of the PBP activities include dd-transpeptidase and dd-carboxypeptidase activities, which carry out the cross-linking of the cell wall and trimming of the peptidoglycan, the major constituent of the cell wall, by an amino acid, respectively. The activity of the latter enzyme moderates the degree of cross-linking of the cell wall, which is carried out by the former. Both these enzymes go through an acyl-enzyme species in the course of their catalytic events. Compound 6, a Cephalosporin Derivative incorporated with structural features of the peptidoglycan was conceived as an inhibitor specific for dd-transpeptidases. On acylation of the active sites of dd-transpeptidases, the molecule would organize itself in the two active site subsites such that it mimics the two sequestered strands of the bacterial peptidoglycan en route to their cross-linking. He...