Binding of Tetrabromobisphenol A and S to Human Serum Albumin Is Weakened by Coexisting Nanoplastics and Environmental Kosmotropes

Zhao, Zongshan; Li, Haimei; Yao, Jiaqiang; Lan, Jing; Bao, Yan; Zhao, Lining; Zong, Wansong; Zhang, Qing; Hollert, Henner; Zhao, Xingchen

doi:10.1021/acs.est.2c09090

Cited by 16 publications

(1 citation statement)

References 41 publications

(64 reference statements)

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“…The results, listed in Table 1, showed that the K SV values were negatively correlated with temperature. The K q values obtained were higher than 2.0 × 10 10 M −1 s −1 [16], indicating that static quenching was the dominant mechanism of BSA quenching with HES 200/0.5, which was initiated by the formation of a complex [17].…”

Section: Resultsmentioning

confidence: 99%

Synthesis of hydroxyethyl starch 200/0.5‐loaded albumin nanoparticles: biocompatibility and interaction mechanism

Zhou

Zhang

et al. 2023

Luminescence

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We aim to synthesize hydroxyethyl starch (HES) 200/0.5 ‐loaded bovine serum albumin nanoparticles (HBNs) and investigate the compatibility and binding mechanism in simulated physiological environments. Herein, to elucidate the morphology, biocompatibility, and formation mechanism of HBNs, techniques such as scanning electron microscopy, hemolysis test, fluorescence, and circular dichroism spectroscopy were applied. The thermodynamic parameters at body temperature (ΔS°=‐26.7 J·mol‐1·K‐1, ΔH°=‐3.20×104 J·mol‐1, and ΔG=‐2.35×104 J·mol‐1,) showed a 1:1 binding stoichiometry, which was formed by hydrogen bonds and van der Waals interactions. Besides, the conformational analysis showed that the microenvironment of fluorophores was altered with the adaptational protein secondary structural changes. Energy transfer occurred from the fluorophores to HES with a high possibility. All these results provided accurate and complete primary data for demonstrating the interaction mechanisms of HES with BSA, which helps understand its pharmaceutical effects in blood.

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Section: Resultsmentioning

confidence: 99%

Synthesis of hydroxyethyl starch 200/0.5‐loaded albumin nanoparticles: biocompatibility and interaction mechanism

Zhou

Zhang

et al. 2023

Luminescence

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Association mechanism of bicalutamide and human serum albumin for potential clinical implications

Wang,

Liu,

Zhang

et al. 2024

Luminescence

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The binding mechanism of molecular interaction between bicalutamide and human serum albumin (HSA) in a pH 7.4 phosphate buffer was studied using various spectroscopic techniques in combination with molecular modeling. Fluorescence data revealed that the fluorescence quenching of HSA by bicalutamide was a static quenching procedure. The binding constants and number of binding sites were evaluated at different temperatures. The thermodynamic parameters, ΔH and ΔS, were calculated to be 4.30 × 104 J·mol−1 and 245 J·mol−1·K−1, respectively, suggesting that the binding of bicalutamide to HSA was driven mainly by hydrophobic interactions and hydrogen bonds. The displacement studies indicated neither Sudlow's site I nor II but subdomain IB as the main binding site for bicalutamide on HSA. The binding distance between bicalutamide and HSA was determined to be 3.54 nm based on the Förster theory. Analysis of circular dichroism, synchronous, and 3D fluorescence spectra demonstrated that HSA conformation was slightly altered in the presence of bicalutamide.

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Binding of Perfluoroalkyl Substances to Nanoplastic Protein Corona Is pH‐Dependent and Attenuates Their Bioavailability and Toxicity

Zhao,

Yao,

et al. 2024

Small Science

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There is a severe lack of understanding of the effects of micro/nanoplastics on human proteins and cells, especially in the presence of organic pollutants. Herein, both in vivo and in vitro assays are conducted to structurally evaluate blood protein complexed with perfluorooctanoic acid (PFOA) and perfluorooctane sulfonate (PFOS) as well as their coronas formed on polystyrene nanoplastics (PNs). PFOS is bound to serum albumin (SA) about 4 times as firmly as PFOA, which is not influenced by protein corona formation onto PN surfaces. However, the small molecular binding dramatically suppresses SA–PN aggregation. Low pH weakens the protein interaction of PFOS while not PFOA, which is also independent of PN adsorption, but the interaction with SA is still stronger for PFOS than PFOA, indicating higher serum persistence and risks. The presence of PN suppresses the cellular uptake of the chemicals and attenuates cytotoxicity due to low bioavailability. Overall, these results provide fundamental information on the ternary interaction mode of protein, particle, and organic pollutants in physiological environments with varying pH, as well as the subsequent cellular responses.

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Binding of Tetrabromobisphenol A and S to Human Serum Albumin Is Weakened by Coexisting Nanoplastics and Environmental Kosmotropes

Cited by 16 publications

References 41 publications

Synthesis of hydroxyethyl starch 200/0.5‐loaded albumin nanoparticles: biocompatibility and interaction mechanism

Synthesis of hydroxyethyl starch 200/0.5‐loaded albumin nanoparticles: biocompatibility and interaction mechanism

Association mechanism of bicalutamide and human serum albumin for potential clinical implications

Binding of Perfluoroalkyl Substances to Nanoplastic Protein Corona Is pH‐Dependent and Attenuates Their Bioavailability and Toxicity

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