Revealing the mechanistic interactions of profenofos and captan pesticides with serum protein via biophysical and computational investigations
Abstract Profenofos (PF) and captan (CT) are among the most utilized organophosphorus insecticides and phthalimide fungicides, respectively. To elucidate the physicochemical and influential toxicokinetic factors, the mechanistic interactions of serum albumin and either PF or CT were carried out in t...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2024-01-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-024-52169-2 |
| _version_ | 1827377370917502976 |
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| author | Kamonrat Phopin Waralee Ruankham Supaluk Prachayasittikul Virapong Prachayasittikul Tanawut Tantimongcolwat |
| author_facet | Kamonrat Phopin Waralee Ruankham Supaluk Prachayasittikul Virapong Prachayasittikul Tanawut Tantimongcolwat |
| author_sort | Kamonrat Phopin |
| collection | DOAJ |
| description | Abstract Profenofos (PF) and captan (CT) are among the most utilized organophosphorus insecticides and phthalimide fungicides, respectively. To elucidate the physicochemical and influential toxicokinetic factors, the mechanistic interactions of serum albumin and either PF or CT were carried out in the current study using a series of spectroscopy and computational analyses. Both PF and CT could bind to bovine serum albumin (BSA), a representative serum protein, with moderate binding constants in a range of 103–104 M−1. The bindings of PF and CT did not induce noticeable BSA’s structural changes. Both pesticides bound preferentially to the site I pocket of BSA, where the hydrophobic interaction was the main binding mode of PF, and the electrostatic interaction drove the binding of CT. As a result, PF and CT may not only induce direct toxicity by themselves, but also compete with therapeutic drugs and essential substances to sit in the Sudlow site I of serum albumin, which may interfere with the pharmacokinetics and equilibrium of drugs and other substances causing consequent adverse effects. |
| first_indexed | 2024-03-08T12:38:11Z |
| format | Article |
| id | doaj.art-2b54a937467c454ba707879a10160fe3 |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-03-08T12:38:11Z |
| publishDate | 2024-01-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-2b54a937467c454ba707879a10160fe32024-01-21T12:17:12ZengNature PortfolioScientific Reports2045-23222024-01-0114111410.1038/s41598-024-52169-2Revealing the mechanistic interactions of profenofos and captan pesticides with serum protein via biophysical and computational investigationsKamonrat Phopin0Waralee Ruankham1Supaluk Prachayasittikul2Virapong Prachayasittikul3Tanawut Tantimongcolwat4Center for Research Innovation and Biomedical Informatics, Faculty of Medical Technology, Mahidol UniversityCenter for Research Innovation and Biomedical Informatics, Faculty of Medical Technology, Mahidol UniversityCenter for Research Innovation and Biomedical Informatics, Faculty of Medical Technology, Mahidol UniversityDepartment of Clinical Microbiology and Applied Technology, Faculty of Medical Technology, Mahidol UniversityCenter for Research Innovation and Biomedical Informatics, Faculty of Medical Technology, Mahidol UniversityAbstract Profenofos (PF) and captan (CT) are among the most utilized organophosphorus insecticides and phthalimide fungicides, respectively. To elucidate the physicochemical and influential toxicokinetic factors, the mechanistic interactions of serum albumin and either PF or CT were carried out in the current study using a series of spectroscopy and computational analyses. Both PF and CT could bind to bovine serum albumin (BSA), a representative serum protein, with moderate binding constants in a range of 103–104 M−1. The bindings of PF and CT did not induce noticeable BSA’s structural changes. Both pesticides bound preferentially to the site I pocket of BSA, where the hydrophobic interaction was the main binding mode of PF, and the electrostatic interaction drove the binding of CT. As a result, PF and CT may not only induce direct toxicity by themselves, but also compete with therapeutic drugs and essential substances to sit in the Sudlow site I of serum albumin, which may interfere with the pharmacokinetics and equilibrium of drugs and other substances causing consequent adverse effects.https://doi.org/10.1038/s41598-024-52169-2 |
| spellingShingle | Kamonrat Phopin Waralee Ruankham Supaluk Prachayasittikul Virapong Prachayasittikul Tanawut Tantimongcolwat Revealing the mechanistic interactions of profenofos and captan pesticides with serum protein via biophysical and computational investigations Scientific Reports |
| title | Revealing the mechanistic interactions of profenofos and captan pesticides with serum protein via biophysical and computational investigations |
| title_full | Revealing the mechanistic interactions of profenofos and captan pesticides with serum protein via biophysical and computational investigations |
| title_fullStr | Revealing the mechanistic interactions of profenofos and captan pesticides with serum protein via biophysical and computational investigations |
| title_full_unstemmed | Revealing the mechanistic interactions of profenofos and captan pesticides with serum protein via biophysical and computational investigations |
| title_short | Revealing the mechanistic interactions of profenofos and captan pesticides with serum protein via biophysical and computational investigations |
| title_sort | revealing the mechanistic interactions of profenofos and captan pesticides with serum protein via biophysical and computational investigations |
| url | https://doi.org/10.1038/s41598-024-52169-2 |
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