Kabir, Md. Zahirul and Seng, Jane and Mohamad, Saharuddin B. and Gülsüm Bilgiç, Merve and Uslu, Bengi (2024) Exploration of the intermolecular isoproturon–bovine serum albumin combination: Biophysical and computational prospects. Journal of Photochemistry and Photobiology A: Chemistry, 450. ISSN 1010-6030, DOI https://doi.org/10.1016/j.jphotochem.2024.115464.
Full text not available from this repository.Abstract
Isoproturon (IPU), a selective systemic herbicide that is frequently applied to eradicate large-leaved weeds and annual grasses in agricultural fields. However, the accumulation of IPU residues during food production might negatively affect on human and animal health. To comprehend the impact of IPU on the mankind and environment, the interaction analysis of IPU with plasma protein is crucial. This work used a variety of techniques, including fluorescence, UV–vis absorption, computational docking and dynamics simulation to extensively examine the combination of IPU with bovine serum albumin (BSA) under typical physiological settings. IPU quenched the BSA fluorescence and form the IPU–BSA complex through a static process. A weak binding affinity was anticipated (binding constant = 4.68–2.48 × 103 M−1) for IPU–BSA interaction. Thermodynamic results revealed that the IPU–BSA binding reaction was a spontaneous process, predominantly governed by hydrogen bonds, van der Waals and hydrophobic forces, which was well supported by molecular docking analysis. Synchronous and three-dimensional fluorescence spectral results exhibited microenvironmental fluctuations near the protein's Trp and Tyr residues with added IPU, but inclusion of IPU to BSA was observed to enhance the protein's thermal constancy. Site marker displacement results demonstrated that IPU desirably binds to BSA at site II. An in silico findings also unveiled the primary binding arrangement of IPU was placed at site II of BSA and surrounded by hydrophobic and polar residues. Molecular dynamics simulation results suggested the IPU–BSA complex persisted compact and stable. © 2024 Elsevier B.V.
| Item Type: | Article |
|---|---|
| Funders: | TUBITAK-2209-A Uni-versity Students Research Projects Support Program |
| Uncontrolled Keywords: | Binding energy; Fluorescence; Hydrogen bonds; Hydrophobicity; Mammals; Molecular dynamics; Molecular modeling; Proteins; Reaction kinetics; Surface plasmon resonance; Van der Waals forces; Weed control; Agricultural fields; Animal health; Annual grass; Bovine serum albumins; Dynamics simulation; Food production; Human health; Isoproturon; Molecular docking; Serum albumin; Herbicides |
| Subjects: | Q Science > QD Chemistry |
| Divisions: | Faculty of Science > Institute of Biological Sciences |
| Depositing User: | Ms. Juhaida Abd Rahim |
| Date Deposited: | 11 Jul 2024 04:23 |
| Last Modified: | 11 Jul 2024 04:23 |
| URI: | http://eprints.um.edu.my/id/eprint/44744 |
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