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    Vancomycin derivatives that inhibit peptidoglycan biosynthesis without binding D-Ala-D-Ala (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-04-16
    Description: Vancomycin is an important drug for the treatment of Gram-positive bacterial infections. Resistance to vancomycin has begun to appear, posing a serious public health threat. Vancomycin analogs containing modified carbohydrates are very active against resistant microorganisms. Results presented here show that these carbohydrate derivatives operate by a different mechanism than vancomycin; moreover, peptide binding is not required for activity. It is proposed that carbohydrate-modified vancomycin compounds are effective against resistant bacteria because they interact directly with bacterial proteins involved in the transglycosylation step of cell wall biosynthesis. These results suggest new strategies for designing glycopeptide antibiotics that overcome bacterial resistance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ge, M -- Chen, Z -- Onishi, H R -- Kohler, J -- Silver, L L -- Kerns, R -- Fukuzawa, S -- Thompson, C -- Kahne, D -- New York, N.Y. -- Science. 1999 Apr 16;284(5413):507-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Princeton University Princeton, NJ 08544, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10205063" target="_blank"〉PubMed〈/a〉
    Keywords: Anti-Bacterial Agents/chemistry/metabolism/*pharmacology ; Carbohydrates/chemistry ; Cell Membrane/metabolism ; Dipeptides/*metabolism ; Drug Design ; Drug Resistance, Microbial ; Enterococcus faecalis/drug effects ; Escherichia coli/drug effects/metabolism ; Glycosylation ; Hexosyltransferases/antagonists & inhibitors/metabolism ; Lipid Metabolism ; Microbial Sensitivity Tests ; Peptidoglycan/*biosynthesis ; Peptidoglycan Glycosyltransferase ; Protein Binding ; Protein Precursors/metabolism ; Structure-Activity Relationship ; Vancomycin/*analogs & derivatives/chemistry/metabolism/*pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Antibacterial agents that inhibit lipid A biosynthesis (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-08
    Description: Lipid A constitutes the outer monolayer of the outer membrane of Gram-negative bacteria and is essential for bacterial growth. Synthetic antibacterials were identified that inhibit the second enzyme (a unique deacetylase) of lipid A biosynthesis. The inhibitors are chiral hydroxamic acids bearing certain hydrophobic aromatic moieties. They may bind to a metal in the active site of the deacetylase. The most potent analog (with an inhibition constant of about 50 nM) displayed a minimal inhibitory concentration of about 1 microgram per milliliter against Escherichia coli, caused three logs of bacterial killing in 4 hours, and cured mice infected with a lethal intraperitoneal dose of E. coli.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Onishi, H R -- Pelak, B A -- Gerckens, L S -- Silver, L L -- Kahan, F M -- Chen, M H -- Patchett, A A -- Galloway, S M -- Hyland, S A -- Anderson, M S -- Raetz, C R -- New York, N.Y. -- Science. 1996 Nov 8;274(5289):980-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Merck Research Laboratories, Rahway, NJ 07065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8875939" target="_blank"〉PubMed〈/a〉
    Keywords: Amidohydrolases/*antagonists & inhibitors/metabolism ; Animals ; Anti-Bacterial Agents/chemistry/*pharmacology ; Binding Sites ; Escherichia coli/drug effects ; Escherichia coli Infections/drug therapy ; Gram-Negative Bacteria/*drug effects ; Hydroxamic Acids/chemistry/*pharmacology ; Lipid A/*biosynthesis ; Mice ; Microbial Sensitivity Tests ; Oxazoles/chemistry/pharmacology ; Pseudomonas/drug effects ; Serratia/drug effects ; Stereoisomerism ; Structure-Activity Relationship
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
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    PAPER CURRENT
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