Source:http://linkedlifedata.com/resource/pubmed/id/11480890
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2001-8-1
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pubmed:abstractText |
A series of hydrophobic N'-mono and N',N"-double alkylated derivatives of the glycopeptide antibiotic eremomycin were synthesized by reductive alkylation after preliminary protection of the N-terminal amino group of the peptide backbone. The investigation of the antibacterial activity in vitro showed that N'-C10H21- and N'-p-(p-chlorophenyl)benzyl derivatives of eremomycin are the most active against vancomycin-resistant enterococci among the compounds obtained though they are less effective than the corresponding lipophilic derivatives of vancomycin. The introduction of two hydrophobic substituents led to a decrease in activity against both susceptible and resistant bacteria. The biochemical evaluation of the mode of action revealed that in addition to binding to D-Ala-D-Ala these compounds also have an alternative mechanism of action that does not require substrate binding.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-8820
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
54
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
455-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11480890-Alkylation,
pubmed-meshheading:11480890-Anti-Bacterial Agents,
pubmed-meshheading:11480890-Cell Wall,
pubmed-meshheading:11480890-Drug Resistance, Microbial,
pubmed-meshheading:11480890-Enterococcus,
pubmed-meshheading:11480890-Glycopeptides,
pubmed-meshheading:11480890-Glycosylation,
pubmed-meshheading:11480890-Microbial Sensitivity Tests,
pubmed-meshheading:11480890-Structure-Activity Relationship,
pubmed-meshheading:11480890-Surface Properties,
pubmed-meshheading:11480890-Vancomycin
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pubmed:year |
2001
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pubmed:articleTitle |
Synthesis of hydrophobic N'-mono and N',N"-double alkylated eremomycins inhibiting the transglycosylation stage of bacterial cell wall biosynthesis.
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pubmed:affiliation |
Institute of New Antibiotics of the Russian Academy of Medical Sciences, Moscow.
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pubmed:publicationType |
Journal Article,
Comparative Study
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