Comprehensive insights into the interactions of dicyclohexyl phthalate and its metabolite to human serum albumin

Lv, Xiaolan; Jiang, Zheng; Zeng, Guofang; Zhao, Sujuan; Li, Na; Chen, Fengping; Huang, Xiaojian; Jia, Yinhua; Tuo, Xun

doi:10.1016/j.fct.2021.112407

Cited by 32 publications

(12 citation statements)

References 75 publications

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“…The appearance of the blue-green dots indicated by the yellow arrows suggested that the driving forces for PAEs-DNase I binding were van der Waals forces and hydrogen bonds. This result was consistent with the binding force analysis results of PAEs binding with human serum albumin (HSA) (Lv et al 2021). Additionally, 1 ~ 3 hydrogen bonds were formed during the binding process.…”

Section: Resultssupporting

confidence: 90%

The binding of phthalates with nuclease influences the DNA enzymatic degradation

Qin

Cheng

Yang

et al. 2022

Preprint

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Extracellular DNA (exDNA) degradation determines the persistence and the dissemination of antibiotic resistance genes which are the root cause for antibiotic resistance threatened human health. However, the effect of ubiquitous environmental endocrine-disrupting chemicals such as phthalates (PAEs) on this process is unclear. Here, we investigated the DNA degradation in the presence of five typical PAEs [dimethyl phthalate (DMP), diethyl phthalate (DEP), dibutyl phthalate (DBP), bis(2-ethylhexyl) phthalate (DEHP), benzyl butyl phthalate (BBP)] via gel electrophoresis experiments, spectroscopic analyses, atomic force microscopy, and molecular dynamics simulations. Results show that the PAEs inhibited DNA enzymatic degradation. PAEs were bound to amino groups in deoxyribonuclease I (DNase I) amino acid residues via van der Waals forces and hydrogen bonding, leading to the decrease of helix structure and structural deformation of DNase I, which in turn caused the decrease of its enzymatic activity. This binding interaction mainly contributed to the inhibition of DNA degradation. The maximum inhibition rates of PAEs on DNase I enzymatic activity were up to 83% (DMP), 64% (DEP), 60% (DBP), 77% (DEHP), 88% (BBP), respectively. This work provides interesting insights into how coexistent toxic organic contaminants affect the environmental fate of genetic macromolecules and further reveals their molecular ecological effects.

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Section: Resultssupporting

confidence: 90%

The binding of phthalates with nuclease influences the DNA enzymatic degradation

Qin

Cheng

Yang

et al. 2022

Preprint

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“…As listed in Table 1, at 293 K, the K b values of the 1‐OHPhe–HSA and 1‐OHPhe–BSA systems were 2.08 × 10 4 and 1.25 × 10 5 L mol −1 , respectively, whereas those of the 9‐OHPhe–HSA and 9‐OHPhe–BSA systems were 8.74 × 10 4 and 1.24 × 10 4 L mol −1 , respectively. The binding affinities of the two serum albumins for 1‐OHPhe and 9‐OHPhe are comparable with those of pollutants, such as phenanthrene (1.19 × 10 5 L mol −1 ), [ 41 ] and dicyclohexyl phthalate (3.95 × 10 5 L mol −1 ), [ 35 ] and drugs, such as nicotinamide (3.25 × 10 5 L mol −1 ) [ 52 ] and ibuprofen (7.07 × 10 4 L mol −1 ), [ 53 ] which were measured in vitro under simulated physiological conditions. These results suggest that the binding affinity of HSA was weaker than that of BSA for 1‐OHPhe, but stronger than that of BSA for 9‐OHPhe.…”

Section: Resultsmentioning

confidence: 98%

“…The spectrofluorimetric characteristics of protein fluorophores are sensitive to changes in the protein structure and microenvironment. [ 35 ] Therefore, the fluorescence quenching method was used to elucidate the binding mechanism between OH‐PAHs and serum albumins. [ 36 ] To obtain the spectral characteristics of each target, the three‐dimensional (3D) fluorescence spectra of 1‐OHPhe, 9‐OHPhe, BSA, and HSA were measured.…”

Section: Resultsmentioning

confidence: 99%

Interactions between hydroxylated polycyclic aromatic hydrocarbons and serum albumins: multispectral and molecular docking analyses

Zhang

Zhu

et al. 2022

Luminescence

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Hydroxylated polycyclic aromatic hydrocarbons (OH‐PAHs) can bind to serum albumin and influence their distribution and elimination in organisms. Here, multispectral analysis and molecular docking methods were used to investigate the binding mechanism of two OH‐PAHs, 1‐hydroxyphenanthrene (1‐OHPhe) and 9‐hydroxyphenanthrene (9‐OHPhe), with two homologous serum albumins, human serum albumin (HSA) and bovine serum albumin (BSA). The quenching constants of HSA with 1‐OHPhe and 9‐OHPhe were much larger than those for BSA. Energy transfer from the tryptophan (Trp) residues in HSA to 1‐OHPhe and 9‐OHPhe was more probable than from Trp in BSA. The interactions of 1‐OHPhe and 9‐OHPhe with Trp in HSA and BSA altered the microenvironment of Trp. Molecular docking results revealed that the binding modes and binding forces of 1‐OHPhe and 9‐OHPhe with HSA and BSA were different. The two OH‐PAHs were used as fluorescent probes to analyze the microenvironmental hydrophobicities of HSA and BSA, which were distinctly different. The structural difference between HSA and BSA induced significant variations in their binding behaviour with 1‐OHPhe and 9‐OHPhe. Moreover, HSA was more susceptible to 1‐OHPhe and 9‐OHPhe than BSA. This work suggests that the differences between the two serum albumins should be considered in related studies.

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“…The binding affinity from weak to medium is attributed to K a values in the range 10 2 –10 4 M −1 . [ 49 ] According to the data listed in Table 3, the n values indicated that there was nearly one binding site between BLC and NDP. K a values at four temperatures were all larger than 10 4 M −1 and decreased with increasing temperatures, which indicated that the interaction occurred between NDP and BLC.…”

Section: Resultsmentioning

confidence: 99%

Elucidation on inhibition and binding mechanism of bovine liver catalase by nifedipine: multispectroscopic analysis and computer simulation methods

Zhou

Xiao

et al. 2022

Luminescence

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Nifedipine (NDP), a dihydropyridine calcium antagonist, is widely used for the treatment of hypertension and angina pectoris. Catalase is a key antioxidant enzyme that is closely relevant to the level of reactive oxygen specie in vivo. Here, the research explored the effects of NDP on the conformation and catalytic function of bovine liver catalase (BLC) through enzymatic reaction kinetic techniques, multispectroscopic analysis, and computer simulation methods. Kinetic studies clarified that the NDP reduced the activity of BLC using a noncompetitive inhibition mechanism.Based on trial data, a static quenching mechanism functioned in quenching the intrinsic fluorescence of BLC. The binding constant value was (4.486 ± 0.008) Â 10 4 M À1 (298 K) and BLC had one binding site for NDP. Tyr was prone to be exposed more to a hydrophilic environment in wake of a shift in fluorescence value. The binding reaction of BLC to NDP caused a conformational change in BLC, which in turn led to

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Comprehensive insights into the interactions of dicyclohexyl phthalate and its metabolite to human serum albumin

Cited by 32 publications

References 75 publications

The binding of phthalates with nuclease influences the DNA enzymatic degradation

The binding of phthalates with nuclease influences the DNA enzymatic degradation

Interactions between hydroxylated polycyclic aromatic hydrocarbons and serum albumins: multispectral and molecular docking analyses

Elucidation on inhibition and binding mechanism of bovine liver catalase by nifedipine: multispectroscopic analysis and computer simulation methods

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