Spectroscopic Analysis of the Binding of Paraquat and Diquat Herbicides to Biosubstrates
The study of the interaction of persistent organic pollutants with biosubstrates helps to unravel the pathways for toxicity, however, few mechanistic data are present in the literature for these systems. We analyzed the binding of paraquat (PQ) and diquat (DQ) herbicides to natural calf thymus DNA a...
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doaj-23144bacd7ac46b484db2b5c3b02ba742021-03-03T00:01:16ZengMDPI AGInternational Journal of Environmental Research and Public Health1661-78271660-46012021-03-01182412241210.3390/ijerph18052412Spectroscopic Analysis of the Binding of Paraquat and Diquat Herbicides to BiosubstratesFrancesca Macii0Rebecca Detti1Francesca Rita Bloise2Stefania Giannarelli3Tarita Biver4Department of Chemistry and Industrial Chemistry, University of Pisa, 56124 Pisa, ItalyDepartment of Chemistry and Industrial Chemistry, University of Pisa, 56124 Pisa, ItalyDepartment of Chemistry and Industrial Chemistry, University of Pisa, 56124 Pisa, ItalyDepartment of Chemistry and Industrial Chemistry, University of Pisa, 56124 Pisa, ItalyDepartment of Chemistry and Industrial Chemistry, University of Pisa, 56124 Pisa, ItalyThe study of the interaction of persistent organic pollutants with biosubstrates helps to unravel the pathways for toxicity, however, few mechanistic data are present in the literature for these systems. We analyzed the binding of paraquat (PQ) and diquat (DQ) herbicides to natural calf thymus DNA and a DNA G-quadruplex by spectrophotometric titrations, ethidium bromide exchange tests, viscometry, and melting experiments. The interaction with bovine serum albumin (BSA) protein was studied spectrofluorimetrically at different temperatures. The retention of the targets on positive, negative, and neutral micellar aggregates and liposomes was analyzed by ultrafiltration experiments. Despite some favorable features, PQ and DQ only externally bind natural DNA and do not interact with DNA oligonucleotides. Both herbicides bind bovine serum albumin (BSA). PQ binds BSA mainly according to an electrostatics-driven process. However, ultrafiltration data also show that some hydrophobic contribution participates in the features of these systems. The practical problems related to unfavorable spectroscopic signals and inner filter effects are also discussed. Overall, both herbicides show a low affinity for nucleic acids and weak penetration into liposomes; in addition, the equilibrium constants values found for BSA system suggest optimal conditions for transport in the body.https://www.mdpi.com/1660-4601/18/5/2412intercalationexternal bindingtransportinner filter effectmicellesliposomes |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Francesca Macii Rebecca Detti Francesca Rita Bloise Stefania Giannarelli Tarita Biver |
spellingShingle |
Francesca Macii Rebecca Detti Francesca Rita Bloise Stefania Giannarelli Tarita Biver Spectroscopic Analysis of the Binding of Paraquat and Diquat Herbicides to Biosubstrates International Journal of Environmental Research and Public Health intercalation external binding transport inner filter effect micelles liposomes |
author_facet |
Francesca Macii Rebecca Detti Francesca Rita Bloise Stefania Giannarelli Tarita Biver |
author_sort |
Francesca Macii |
title |
Spectroscopic Analysis of the Binding of Paraquat and Diquat Herbicides to Biosubstrates |
title_short |
Spectroscopic Analysis of the Binding of Paraquat and Diquat Herbicides to Biosubstrates |
title_full |
Spectroscopic Analysis of the Binding of Paraquat and Diquat Herbicides to Biosubstrates |
title_fullStr |
Spectroscopic Analysis of the Binding of Paraquat and Diquat Herbicides to Biosubstrates |
title_full_unstemmed |
Spectroscopic Analysis of the Binding of Paraquat and Diquat Herbicides to Biosubstrates |
title_sort |
spectroscopic analysis of the binding of paraquat and diquat herbicides to biosubstrates |
publisher |
MDPI AG |
series |
International Journal of Environmental Research and Public Health |
issn |
1661-7827 1660-4601 |
publishDate |
2021-03-01 |
description |
The study of the interaction of persistent organic pollutants with biosubstrates helps to unravel the pathways for toxicity, however, few mechanistic data are present in the literature for these systems. We analyzed the binding of paraquat (PQ) and diquat (DQ) herbicides to natural calf thymus DNA and a DNA G-quadruplex by spectrophotometric titrations, ethidium bromide exchange tests, viscometry, and melting experiments. The interaction with bovine serum albumin (BSA) protein was studied spectrofluorimetrically at different temperatures. The retention of the targets on positive, negative, and neutral micellar aggregates and liposomes was analyzed by ultrafiltration experiments. Despite some favorable features, PQ and DQ only externally bind natural DNA and do not interact with DNA oligonucleotides. Both herbicides bind bovine serum albumin (BSA). PQ binds BSA mainly according to an electrostatics-driven process. However, ultrafiltration data also show that some hydrophobic contribution participates in the features of these systems. The practical problems related to unfavorable spectroscopic signals and inner filter effects are also discussed. Overall, both herbicides show a low affinity for nucleic acids and weak penetration into liposomes; in addition, the equilibrium constants values found for BSA system suggest optimal conditions for transport in the body. |
topic |
intercalation external binding transport inner filter effect micelles liposomes |
url |
https://www.mdpi.com/1660-4601/18/5/2412 |
work_keys_str_mv |
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