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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
15
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pubmed:dateCreated |
2008-6-16
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pubmed:abstractText |
Gramicidin S, a cationic cyclic decapeptide, exhibits the potent antibiotic activity through perturbation of lipid bilayers of the bacterial membrane. From the screening of natural antibiotics, we identified gramicidin S as a potent inhibitor for cytochrome bd-type quinol oxidase from Escherichia coli. We found that gramicidin S inhibited the oxidase with IC(50) of 3.5 microM by decreasing V(max) and the affinity for substrates but showed the stimulatory effect at low concentrations. Our findings would provide a new insight into the development of gramicidin S analogs, which do not share the target and mechanism with conventional antibiotics.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
582
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2299-302
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pubmed:meshHeading |
pubmed-meshheading:18519036-Anti-Bacterial Agents,
pubmed-meshheading:18519036-Cell Membrane,
pubmed-meshheading:18519036-Cytochromes,
pubmed-meshheading:18519036-Detergents,
pubmed-meshheading:18519036-Electron Transport Chain Complex Proteins,
pubmed-meshheading:18519036-Enzyme Inhibitors,
pubmed-meshheading:18519036-Escherichia coli,
pubmed-meshheading:18519036-Escherichia coli Proteins,
pubmed-meshheading:18519036-Gramicidin,
pubmed-meshheading:18519036-Inhibitory Concentration 50,
pubmed-meshheading:18519036-Micelles,
pubmed-meshheading:18519036-Models, Chemical,
pubmed-meshheading:18519036-Oxidoreductases
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pubmed:year |
2008
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pubmed:articleTitle |
Gramicidin S identified as a potent inhibitor for cytochrome bd-type quinol oxidase.
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pubmed:affiliation |
Department of Biomedical Chemistry, Graduate School of Medicine, The University of Tokyo, Bunkyo-ku, Tokyo, Japan. tmogi@m.u-tokyo.ac.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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