| dc.contributor.author |
Chronopoulou, EG |
en |
| dc.contributor.author |
Papageorgiou, AC |
en |
| dc.contributor.author |
Markoglou, A |
en |
| dc.contributor.author |
Labrou, NE |
en |
| dc.date.accessioned |
2014-06-06T06:51:52Z |
|
| dc.date.available |
2014-06-06T06:51:52Z |
|
| dc.date.issued |
2012 |
en |
| dc.identifier.issn |
13811177 |
en |
| dc.identifier.uri |
http://dx.doi.org/10.1016/j.molcatb.2012.04.022 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/5744 |
|
| dc.subject |
Glutathione transferase |
en |
| dc.subject |
In silico molecular docking |
en |
| dc.subject |
Pesticide determination |
en |
| dc.subject |
Xenobiotics |
en |
| dc.subject.other |
Detoxification mechanism |
en |
| dc.subject.other |
Glutathione transferase |
en |
| dc.subject.other |
In-phase |
en |
| dc.subject.other |
In-silico |
en |
| dc.subject.other |
Linear calibration curve |
en |
| dc.subject.other |
Molecular docking |
en |
| dc.subject.other |
Relative standard deviations |
en |
| dc.subject.other |
Reproducibilities |
en |
| dc.subject.other |
Sample preparation |
en |
| dc.subject.other |
Water samples |
en |
| dc.subject.other |
Xenobiotics |
en |
| dc.subject.other |
Assays |
en |
| dc.subject.other |
Biochemistry |
en |
| dc.subject.other |
Insecticides |
en |
| dc.subject.other |
Isoenzymes |
en |
| dc.subject.other |
Peptides |
en |
| dc.subject.other |
Enzyme inhibition |
en |
| dc.subject.other |
dieldrin |
en |
| dc.subject.other |
glutathione transferase |
en |
| dc.subject.other |
glutathione transferase A1 |
en |
| dc.subject.other |
glutathione transferase O1 |
en |
| dc.subject.other |
glutathione transferase P1 |
en |
| dc.subject.other |
glutathione transferase T2 |
en |
| dc.subject.other |
insecticide |
en |
| dc.subject.other |
spiromesifen |
en |
| dc.subject.other |
unclassified drug |
en |
| dc.subject.other |
water |
en |
| dc.subject.other |
analytic method |
en |
| dc.subject.other |
article |
en |
| dc.subject.other |
controlled study |
en |
| dc.subject.other |
drug binding |
en |
| dc.subject.other |
drug determination |
en |
| dc.subject.other |
drug potency |
en |
| dc.subject.other |
enzyme activity |
en |
| dc.subject.other |
enzyme analysis |
en |
| dc.subject.other |
enzyme inhibition |
en |
| dc.subject.other |
IC 50 |
en |
| dc.subject.other |
molecular docking |
en |
| dc.subject.other |
nonhuman |
en |
| dc.title |
Inhibition of human glutathione transferases by pesticides: Development of a simple analytical assay for the quantification of pesticides in water |
en |
| heal.type |
journalArticle |
en |
| heal.identifier.primary |
10.1016/j.molcatb.2012.04.022 |
en |
| heal.publicationDate |
2012 |
en |
| heal.abstract |
Glutathione transferases (GSTs; EC 2.5.1.18) form a group of multifunctional enzymes that are involved in phase II cellular detoxification mechanism. Here, screening of the inhibition potency of a wide range of pesticides toward selected human GST isoenzymes (hGSTA1-1, hGSTP1-1, hGSTT2-2 and hGSTO1-1) was carried out. hGSTA1-1 was found more susceptible to inhibition by pesticides than other isoenzymes. The insecticides dieldrin and spiromesifen were identified as potent reversible inhibitors toward hGSTA1-1 with IC 50 values equal to 17.9 ± 1.7 μM and 12.1 ± 3.4 μM, respectively. Based on in silico docking analysis and kinetic inhibition studies it was concluded that dieldrin and spiromesifen bind specifically to the enzyme presumably at a distinct position that partially overlaps with both the G- and H-site. The ability of dieldrin and spiromesifen to inhibit hGSTA1-1 activity was exploited for the development of analytical quantification assays for these two pesticides. Linear calibration curves were obtained for dieldrin and spiromesifen, with useful concentration in the range of 0-10 μM. The reproducibility of the assay response, expressed by relative standard deviation, was in the order of 4.1% (N = 28). The method was successfully applied to the determination of these pesticides in real water samples without sample preparation steps. © 2012 Elsevier B.V. All rights reserved. |
en |
| heal.journalName |
Journal of Molecular Catalysis B: Enzymatic |
en |
| dc.identifier.volume |
81 |
en |
| dc.identifier.doi |
10.1016/j.molcatb.2012.04.022 |
en |
| dc.identifier.spage |
43 |
en |
| dc.identifier.epage |
51 |
en |