Analyzing organophosphate pesticide-serum albumin binding interaction: a combined STD NMR and molecular docking study
24 Mar 2021-Journal of Biomolecular Structure & Dynamics (Taylor & Francis)-Vol. 39, Iss: 5, pp 1865-1878
TL;DR: In Vitro analysis of the interaction of organophosphate pesticides (OP) with bovine serum albumin (BSA) is crucial to understand their potential effects at the molecular level and Saturation Transfer Difference NMR experiments in conjunction with molecular docking studies revealed a high binding affinity of OP-BSA complexes through non-covalent interaction.
Abstract: In Vitro analysis of the interaction of organophosphate pesticides (OP) with bovine serum albumin (BSA) is crucial to understand their potential effects at the molecular level. In this context, we ...
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TL;DR: In this article, a review of OPC-based enzymes is presented, including their structural differences and identity, mechanisms, and specificity of catalytic action, including results of computational modeling.
Abstract: Organophosphorus compounds (OPCs) are able to interact with various biological targets in living organisms, including enzymes. The binding of OPCs to enzymes does not always lead to negative consequences for the body itself, since there are a lot of natural biocatalysts that can catalyze the chemical transformations of the OPCs via hydrolysis or oxidation/reduction and thereby provide their detoxification. Some of these enzymes, their structural differences and identity, mechanisms, and specificity of catalytic action are discussed in this work, including results of computational modeling. Phylogenetic analysis of these diverse enzymes was specially realized for this review to emphasize a great area for future development(s) and applications.
12 citations
TL;DR: The experimental and computational results have provided the binding affinity, binding mode, conformational flexibility, and thermodynamic profile of Formetanate Hydrochloride (FMT)-HSA complex as mentioned in this paper .
6 citations
TL;DR: In this paper, the role of intermolecular interactions, specifically halogen and chalcogen bonds, in EDC recognition processes is discussed, with an overview of the latest advances in the study of disruption mechanisms.
Abstract: Endocrine-disrupting chemicals (EDCs) are natural or synthetic substances able to mimic, interfere with, or block endogenous hormones, thus disrupting the normal function of the endocrine system Most of them are largely applied in agriculture and industry As a result, humans are chronically exposed to mixtures of EDCs Their adverse effect on human health may appear long after exposure, making it difficult to assess their full impact Thus, understanding the molecular basis of recognition of suspected EDCs by their biological targets is fundamental to get insight into their mechanism of action This review will focus on the role of intermolecular interactions, specifically halogen and chalcogen bonds, in EDC recognition processes, offering an overview of the latest advances in the study of disruption mechanisms
6 citations
TL;DR: A modern view on the molecular pathophysiological mechanisms of acute nephrotoxicity of organophosphate compounds is presented.
Abstract: Organophosphates (OPs) are toxic chemicals produced by an esterification process and some other routes. They are the main components of herbicides, pesticides, and insecticides and are also widely used in the production of plastics and solvents. Acute or chronic exposure to OPs can manifest in various levels of toxicity to humans, animals, plants, and insects. OPs containing insecticides were widely used in many countries during the 20th century, and some of them continue to be used today. In particular, 36 OPs have been registered in the USA, and all of them have the potential to cause acute and sub-acute toxicity. Renal damage and impairment of kidney function after exposure to OPs, accompanied by the development of clinical manifestations of poisoning back in the early 1990s of the last century, was considered a rare manifestation of their toxicity. However, since the beginning of the 21st century, nephrotoxicity of OPs as a manifestation of delayed toxicity is the subject of greater attention of researchers. In this article, we present a modern view on the molecular pathophysiological mechanisms of acute nephrotoxicity of organophosphate compounds.
4 citations
TL;DR: In this article, the authors used proton nuclear magnetic resonance (1H NMR) to study the true esterase activity of albumin, using the example of bovine serum albumin (BSA) and p-nitrophenyl acetate (NPA).
Abstract: Serum albumin possesses esterase and pseudo-esterase activities towards a number of endogenous and exogenous substrates, but the mechanism of interaction of various esters and other compounds with albumin is still unclear. In the present study, proton nuclear magnetic resonance (1H NMR) has been applied to the study of true esterase activity of albumin, using the example of bovine serum albumin (BSA) and p-nitrophenyl acetate (NPA). The site of BSA esterase activity was then determined using molecular modelling methods. According to the data obtained, the accumulation of acetate in the presence of BSA in the reaction mixture is much more intense as compared with the spontaneous hydrolysis of NPA, which indicates true esterase activity of albumin towards NPA. Similar results were obtained for p-nitophenyl propionate (NPP) as substrate. The rate of acetate and propionate release confirms the assumption that there is a site of true esterase activity in the albumin molecule, which is different from the site of the pseudo-esterase activity Sudlow II. The results of molecular modelling of BSA and NPA interaction make it possible to postulate that Sudlow site I is the site of true esterase activity of albumin.
1 citations
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TL;DR: In vivo pharmacokinetics of 3,5,6-trichloro-2-pyridinol (TCPy), the major chemical-specific metabolite of CPF, was quantitatively evaluated in rat saliva and results suggest that saliva TCPy concentration can be utilized to ascertain CPF exposure.
21 citations
TL;DR: The interaction of methyl-parathion with the albumin of Piaractus mesopotamicus (= pacu), a fish species typical of Brazilian rivers, was studied and the results compared with known values for human and bovine albumin obtained in an earlier investigation.
Abstract: The interaction of methyl-parathion with the albumin of Piaractus mesopotamicus (Holmberg 1887) (= pacu), a fish species typical of Brazilian rivers, was studied and the results compared with known values for human and bovine albumin obtained in an earlier investigation. Methyl-parathion (O,O-dimethyl O-p-nitrophenyl phosphorothioate) is an organophosphorous pesticide still used in agriculture and fish farming in many countries. The fluorescence quenching technique with tryptophan as a natural probe was used to detect for the presence of methyl-parathion. Fluorescence can be mathematically expressed by the Stern–Volmer equation to calculate quenching constants, and changes in the behavior of Stern–Volmer curves at different temperatures indicate the nature of the mechanism causing the quenching. Our results indicate that methyl-parathion forms a complex with fish albumin. The estimated association constant is 9.73 × 103 (± 4.9 × 102) M−1 at 25°C.
21 citations
Journal Article•
TL;DR: The result suggests that, ibuprofen displaces naproxen and vice versa from its high affinity binding site (site II) and the displaced drug rebounds to its low affinity binding sites (site I) on BSA molecule.
Abstract: The competitive binding characteristics of ibuprofen and naproxen with respect to binding site on bovine serum albumin (BSA) was studied by equilibrium dialysis method at pH 7.4 and 25 degrees C. We studied the effect of one drug on the free concentration of another in vitro during concurrent administration. There was remarkable increase in free concentration of naproxen when ibuprofen (2x10(-5) M) was added to a 1:1 naproxen-BSA mixture (2x10(-5) M: 2x10(-5) M), suggesting that ibuprofen displaced naproxen from its binding sites. However free fraction of naproxen was not increased up to the level expected from direct competitive displacement. Free concentration of ibuprofen was hardly increased by naproxen when naproxen (2x10(-5) M) was added to the ibuprofen-BSA (1:1) mixture. But in both cases, in presence of ranitidine (site I specific probe), the free concentration of the displaced drug increased more prominently compared to that in absence of ranitidine. This result suggests that, ibuprofen displaces naproxen and vice versa from its high affinity binding site (site II) and the displaced drug rebounds to its low affinity binding site (site I) on BSA molecule. This form of modified displacement has been arbitrarily referred to as site-to-site displacement.
20 citations
TL;DR: Deep insights are provided into the direct interaction of the organophosphate metabolites with a biologically important carrier protein, serum albumin, and substantial time-dependent changes in the 1H NMR intensity of PM in the presence of BSA are revealed.
16 citations
TL;DR: Investigation of the interaction between two organophosphate insecticides and bovine serum albumin under physiological conditions and circular dichroism spectroscopy indicates the formation of complex between BSA and the insecticides, a spontaneous process as evidenced by negative free energy changes.
Abstract: The interaction between two organophosphate insecticides (monocrotophos and phosphamidon) and bovine serum albumin (BSA) under physiological conditions is investigated by UV-Vis, fluorescence (steady state, synchronous and three-dimensional) and circular dichroism spectroscopy. The UV-Vis and fluorescence spectral studies indicate the formation of complex between BSA and the insecticides. The complex formation is a spontaneous process as evidenced by negative free energy changes. The positive values of entropy changes reveal that hydrophobic forces played the major role in the interaction process, which is well supported by the molecular docking studies. Synchronous and three-dimensional fluorescence investigations suggest that there is no significant change in the conformation of BSA upon binding with the insecticides, which is strongly supported by the results of circular dichroism spectral studies.
16 citations