rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
16
|
pubmed:dateCreated |
2003-7-22
|
pubmed:abstractText |
Structural modifications to the peptide deformylase inhibitor BB-3497 are described. In this paper, we describe the initial SAR around this lead for modifications to both the P2' and P3' side chains. Enzyme inhibition and antibacterial activity data revealed that a variety of substituents are tolerated at the P2' and P3' positions of the inhibitor backbone. The data from this study highlights the potential for modification at the P2' and P3' positions to optimise the physicochemical properties.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
0960-894X
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
18
|
pubmed:volume |
13
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
2715-8
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:12873500-Amidohydrolases,
pubmed-meshheading:12873500-Amines,
pubmed-meshheading:12873500-Amino Acids,
pubmed-meshheading:12873500-Anti-Bacterial Agents,
pubmed-meshheading:12873500-Bacteria,
pubmed-meshheading:12873500-Enzyme Inhibitors,
pubmed-meshheading:12873500-Escherichia coli,
pubmed-meshheading:12873500-Hydroxamic Acids,
pubmed-meshheading:12873500-Metals,
pubmed-meshheading:12873500-Microbial Sensitivity Tests,
pubmed-meshheading:12873500-Molecular Mimicry,
pubmed-meshheading:12873500-Oligopeptides,
pubmed-meshheading:12873500-Structure-Activity Relationship
|
pubmed:year |
2003
|
pubmed:articleTitle |
Structure--activity relationships of the peptide deformylase inhibitor BB-3497: modification of the P2' and P3' side chains.
|
pubmed:affiliation |
British Biotech Pharmaceuticals Limited, Watlington Road, Oxford OX4 6LY, UK. stephen.davies@evotecoai.com
|
pubmed:publicationType |
Journal Article,
Comparative Study
|