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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2002-11-21
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pubmed:abstractText |
A series of analogues of the potent peptide deformylase (PDF) inhibitor BB-3497 containing alternative metal binding groups was synthesised. Enzyme inhibition and antibacterial activity data for these compounds revealed that the bidentate hydroxamic acid and N-formyl hydroxylamine structural motifs represent the optimum chelating groups on the pseudopeptidic BB-3497 backbone.
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pubmed:language |
eng
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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:author |
pubmed-author:BeckettR PaulRP,
pubmed-author:ClementsJohn MJM,
pubmed-author:DoelSheilaS,
pubmed-author:EastStephen PSP,
pubmed-author:LaunchburySteven BSB,
pubmed-author:PrattLisa MLM,
pubmed-author:SmithHelen KHK,
pubmed-author:SpavoldZoë MZM,
pubmed-author:ThomasWayneW,
pubmed-author:ToddRichard SRS,
pubmed-author:WhittakerMarkM
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3595-9
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pubmed:dateRevised |
2006-11-15
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pubmed:articleTitle |
Structure-activity relationships of the peptide deformylase inhibitor BB-3497: modification of the metal binding group.
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pubmed:affiliation |
British Biotech Pharmaceuticals Limited, Watlington Road, Oxford OX4 6LY, UK.
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