|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
19
|
|
pubmed:dateCreated |
2006-8-25
|
|
pubmed:abstractText |
A series of mono-, di-, and tri-guanidinylated derivatives of neamine were prepared via selective guanidinylation of neamine. These molecules represent a novel scaffold as inhibitors of anthrax lethal factor zinc metalloprotease. Methods for the synthesis of these compounds are described, and structure-activity relationships among the series are analyzed. In addition, initial findings regarding the mechanism of LF inhibition for these molecules are presented.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Oct
|
|
pubmed:issn |
0960-894X
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
1
|
|
pubmed:volume |
16
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
5183-9
|
|
pubmed:dateRevised |
2006-11-15
|
|
pubmed:meshHeading |
pubmed-meshheading:16870442-Aminoglycosides,
pubmed-meshheading:16870442-Antigens, Bacterial,
pubmed-meshheading:16870442-Bacillus anthracis,
pubmed-meshheading:16870442-Bacterial Toxins,
pubmed-meshheading:16870442-Enzyme Inhibitors,
pubmed-meshheading:16870442-Framycetin,
pubmed-meshheading:16870442-Guanidine,
pubmed-meshheading:16870442-Kinetics,
pubmed-meshheading:16870442-Metalloendopeptidases,
pubmed-meshheading:16870442-Structure-Activity Relationship
|
|
pubmed:year |
2006
|
|
pubmed:articleTitle |
Selectively guanidinylated derivatives of neamine. Syntheses and inhibition of anthrax lethal factor protease.
|
|
pubmed:affiliation |
Department of Chemistry, Hawaii Biotech, Inc., 99-193 Aiea Heights Dr., Suite 200, Aiea, 96701, USA. gjiao@hibiotech.com
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
|
