A study on the inhibition of dihydrofolate reductase (DHFR) from Escherichia coli by gold(i) phosphane compounds. X-ray crystal structures of (4,5-dichloro-1H-imidazolate-1-yl)-triphenylphosphane-gold(i) and (4,5-dicyano-1H-imidazolate-1-yl)-triphenylphosphane-gold(i)CCDC 997733 and 997734. For crystallographic data in CIF or other electronic format see DOI: 10.1039/c4dt01542h
An unprecedented study on the inhibitory activities of a class of phosphane gold( i ) complexes on E. coli dihydrofolate reductase (DHFR) is reported. The gold( i ) complexes considered in this work consist of azolate or chloride ligands and phosphane as co-ligands. The ligands have been functionali...
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Main Authors | , , , , , , |
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Format | Journal Article |
Language | English |
Published |
03.02.2015
|
Online Access | Get full text |
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Summary: | An unprecedented study on the inhibitory activities of a class of phosphane gold(
i
) complexes on
E. coli
dihydrofolate reductase (DHFR) is reported. The gold(
i
) complexes considered in this work consist of azolate or chloride ligands and phosphane as co-ligands. The ligands have been functionalized with polar groups (-COOH, -COO
−
, NO
2
, Cl, CN) to obtain better solubility in polar media. Neutral, anionic and cationic gold(
i
) complexes have been tested as DHFR inhibitors by means of a continuous direct spectrophotometric method. X-ray structural characterizations were performed on ((triphenylphosphine)-gold(
i
)-(4,5-dicyanoimidazolyl-1
H
-1yl) and on the analog (triphenylphosphine)-gold(
i
)-(4,5-dichloroimidazolyl-1
H
-1yl). The inhibition constants obtained from the enzyme tests range from 20 μM to 63 nM (auranofin) and are conducive to promoting these compounds as potential DHFR inhibitors.
A study on the inhibition of dihydrofolate reductase (DHFR) by gold(
i
) compounds has been performed. |
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Bibliography: | CCDC 997734 997733 and For crystallographic data in CIF or other electronic format see DOI 10.1039/c4dt01542h |
ISSN: | 1477-9226 1477-9234 |
DOI: | 10.1039/c4dt01542h |