|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
19
|
|
pubmed:dateCreated |
1999-12-17
|
|
pubmed:abstractText |
1,1-Difluoro-2-(tetrahydro-3-furanyl)ethylphosphonic acids cis-3 and trans-3 possessing a N9-purinylmethyl functionality at the ring were synthesized and tested as "multi-substrate analogue" inhibitors for purine nucleoside phosphorylases. Radical cyclization of allyic alpha,alpha-difluorophosphonate (E)-7 was applied to construct the alpha,alpha-difluorophosphonate-functionalized tetrahydrofuranyl moiety. The IC50 values of cis-3 and trans-3 for human erythrocyte PNP-catalyzed phosphorylation of inosine were determined to be 88 and 320 nM, respectively. The stereochemistry of the inhibitors was found to affect significantly the inhibitory potency.
|
|
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 |
4
|
|
pubmed:volume |
9
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
2833-6
|
|
pubmed:dateRevised |
2006-11-15
|
|
pubmed:meshHeading |
pubmed-meshheading:10522701-Antineoplastic Agents,
pubmed-meshheading:10522701-Enzyme Inhibitors,
pubmed-meshheading:10522701-Erythrocytes,
pubmed-meshheading:10522701-Fluorine Compounds,
pubmed-meshheading:10522701-Furans,
pubmed-meshheading:10522701-Gram-Positive Asporogenous Rods,
pubmed-meshheading:10522701-Humans,
pubmed-meshheading:10522701-Inosine,
pubmed-meshheading:10522701-Molecular Structure,
pubmed-meshheading:10522701-Phosphonic Acids,
pubmed-meshheading:10522701-Phosphorylation,
pubmed-meshheading:10522701-Purine-Nucleoside Phosphorylase,
pubmed-meshheading:10522701-Purines
|
|
pubmed:year |
1999
|
|
pubmed:articleTitle |
Synthesis and biological evaluation of 1,1-difluoro-2-(tetrahydro-3-furanyl)ethylphosphonic acids possessing a N9-purinylmethyl functional group at the ring. a new class of inhibitors for purine nucleoside phosphorylases.
|
|
pubmed:affiliation |
School of Pharmacy, Tokyo University of Pharmacy & Life Science, Hachioji, Japan.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
