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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Main Authors: Francesca Macii, Rebecca Detti, Francesca Rita Bloise, Stefania Giannarelli, Tarita Biver
Format: Article
Language:English
Published: MDPI AG 2021-03-01
Series:International Journal of Environmental Research and Public Health
Subjects:
Online Access:https://www.mdpi.com/1660-4601/18/5/2412
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spelling 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 AT francescamacii spectroscopicanalysisofthebindingofparaquatanddiquatherbicidestobiosubstrates
AT rebeccadetti spectroscopicanalysisofthebindingofparaquatanddiquatherbicidestobiosubstrates
AT francescaritabloise spectroscopicanalysisofthebindingofparaquatanddiquatherbicidestobiosubstrates
AT stefaniagiannarelli spectroscopicanalysisofthebindingofparaquatanddiquatherbicidestobiosubstrates
AT taritabiver spectroscopicanalysisofthebindingofparaquatanddiquatherbicidestobiosubstrates
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