JOURNAL OF COORDINATION CHEMISTRY
·
2017
·
IF 1.795
De-Chun Zhang,Dou Ma,Xia Li
Six new coordination complexes, Ln2(2,2′-oba)2(phen)2(ox)(H2O)2 (Ln = Eu 1, Tb 2), Ln4(2,2′-oba)6(phen)2 (Ln = Eu 3, Tb 4), Eu4(2,2′-oba)6(phen)2(H2O) (5), and K[Eu(2,2′-oba)2(phen)2] (6) [2,2′-H2oba = 2,2′-oxybis(benzoic acid), phen = 1,10-phenanthroline, H2ox = oxalic acid] were synthesized by hydrothermal reactions with the same compound molar ratios but different modulatory reagents (MRs). Complexes 1–5 have different 1-D chain structures and 6 shows a mononuclear structure. These complexes form diverse 3-D supramolecular networks through hydrogen bonds. The interaction between these complexes and hippuric acid (HA) or bovine serum albumin (BSA) was investigated by fluorescence spectral analysis. Interestingly, the hippuric acid could quench the luminescence of these complexes while the fluorescence of BSA could be quenched by these complexes. Results suggested that the complexes may be potential luminescent testing reagents for HA or BSA by significant fluorescence quenching of Ln3+ or BSA, respectively, through a static and dynamic quenching process.
研究领域:
化学
·
生物化学
·
材料科学
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DOI
高影响因子
PLoS One
·
2026
·Vol. 21
·期 8
·e0356781
·
IF 2.8
Yan Jiang,Yuhu Feng,Xinyu Li,Bing Zhao,Zuisu Yang,Ruling Wei,Falei Yuan
This study examined the role of bovine serum albumin (BSA) in lipopolysaccharide (LPS)-induced brain injury. Mice were intraperitoneally injected with either LPS or LPS coupled with BSA. Brain tissues were analyzed for autofluorescence, vascular cell permeability, blood-brain barrier integrity, and pyroptosis. Co-immunoprecipitation and immunostaining were performed to assess the interaction between albumin and LPS. The results showed that, compared to the 5 mg/kg LPS group, the 5 mg/kg BSA-LPS group exhibited enhanced autofluorescence and an increased number of cells with co-localization of propidium iodide (PI) with cluster of differentiation 31 (CD31) and CD13. However, no significant differences were observed between the 25 mg/kg LPS and 25 mg/kg BSA-LPS groups. Horseradish peroxidase (HRP) labeling revealed higher HRP leakage in the 5 mg/kg BSA-LPS group compared to the 5 mg/kg LPS group, a difference that disappeared at the 25 mg/kg dose. Peroxidase staining showed a similar trend. Immunostaining for gasdermin D and CD11b showed significant differences only between the 5 mg/kg LPS and 5 mg/kg BSA-LPS groups. CD68 immunostaining exhibited a similar trend. Furthermore, the study confirmed that albumin binds to LPS in the brain, with more abundant Lipid A + signals detected in the 5 mg/kg BSA-LPS group compared to the 5 mg/kg LPS group. These findings collectively suggest that albumin boosts the effect of LPS in the brain, probably by binding with LPS and increasing its entry into the brain parenchyma.
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高影响因子
QUIMICA NOVA
·
2020
·Vol. 43
·期 7
·851-855
·
IF 0.668
Sun Shan,Yuan Zhe,Lu Yuanqi
The primary objective of this study was to investigate the binding of buddleoside to bovine serum albumin (BSA) by different analytical techniques. The analytical principles of affinity capillary electrophoresis (ACE) and fluorescence spectroscopy used in the experiments were different. Mobility (M) that is independent of viscosity of the operating buffer and voltage was chosen to eliminate the effects of electroosmotic flow (EOF) in ACE and was applied to estimate the binding constant Ka. The quenching constant Ksv, binding site number n and binding constant Kb were provided by the fluorescence quenching method. After data analysis of the fluorescence quenching process, it can be seen that the quenching of BSA by buddleoside is a static quenching method. The binding constants between buddleoside and BSA obtained from ACE and fluorescence spectra were 1.218×105 and 1.1915×105, respectively. According to the thermodynamic parameters of ΔG, ΔH and ΔS, it can be inferred that Van Der Waals force and hydrogen bonding force exist in the interaction between buddleoside and BSA. This study can provide a reference for the study of the transport and function mechanism of buddleoside in vivo.
研究领域:
生物化学
·
药学
·
分析化学
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DOI
高影响因子
SCIENCE OF THE TOTAL ENVIRONMENT
·
2022
·
IF 10.753
Jinbin Han,Xiang Qi,Peng Liang
Excess nitrate presented in natural water body and drinking water has been a challenge for maintaining safe ecosystem and human health. Sulfur autotrophic denitrification is proved a feasible technology to remove nitrate from water environment. However, comparatively low rate of sulfur autotrophic denitrification needs to be addressed before wide application of this technology, which is a result of the low solubility of elemental sulfur. Therefore, this study employed bovine serum albumin (BSA) as a supplementary material to modify the elemental sulfur for improved sulfur autotrophic denitrification rate. Artificial biofilm of Thiobacillus denitrificans was prepared and employed in experiments. By testing different amount of BSA applied in both elemental sulfur and the biofilm, including 1 %, 2 % and 4 % mass ratios, it was found that larger employment of BSA had significant effect in increasing the denitrification rate. Particularly when 4 % BSA was added into elemental sulfur, the highest denitrification rate reached 26.8 mg-N/(L·d), 3.7 times of the control group. Meanwhile, the largest reaction rate constant was achieved, 4.13 mg 0.5 /(L 0.5 ·d), 2.78 times of the control group. This effect was attributed to promoted conversion of elemental sulfur to polysulfide that was easily utilized by sulfur-oxidizing bacteria. A long-term operation (14 days) of packed bed reactor filled with sulfur particles and 1 % BSA delivered a much faster start-up than the control and outperformed it with better denitrification performance all-through the experiment. This result evidenced again that BSA could make a highly effective supplement in sulfur autotrophic denitrification.
研究领域:
环境科学
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微生物学
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DOI
PubMed
高影响因子
CARBOHYDRATE POLYMERS
·
2017
·
IF 4.811
Guo Li,Jianying Huang,Tao Chen,Xiangyang Wang,Haijiang Zhang,Qing Chen
Exploiting the uses of proteins and polysaccharides is of increasing interest because the combination of the attributes of these two types of biopolymers can produce small emulsion droplets with good physical stability. The objective of this study was to evaluate the effect of adding chitosan to a bovine serum albumin (BSA) solution at different pH values, and the consequent conformational changes were monitored using UV–vis absorption spectroscopy and fluorescence spectroscopy. Spectroscopic observations were further combined with rheological analysis results to illustrate the interaction mechanism. The results showed that the pH and BSA/chitosan ratio significantly affected the interaction between BSA and chitosan. Additionally, the microenvironment and the secondary structure of BSA were changed with the addition of chitosan, and chitosan was found to quench the intrinsic fluorescence of BSA. The experimental results provide theoretical guidance for the design of new ingredients for the food industry.
研究领域:
食品科学
·
生物化学
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DOI
PubMed
高影响因子
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
·
2018
·
IF 2.88
Hongmei Zhang,Shixin Sun,Yanqing Wang,Zhenghao Fei,Jian Cao
In this work, the interactions between bovine serum albumin (BSA) and five sweeteners including aspartame (APM), acesulfame (AK), sucralose (TGS), sodium cyclamate (SC), and rebaudioside-A (REB-A) have been studied by multispectroscopic techniques, and molecular simulation in order to provide much useful information for the application of new and safer artificial sweeteners. Fluorescence quenching assays indicated that the formation of complexes between sweeteners and BSA mainly induced the fluorescence quenching of protein and the binding site number were about 1 indicting that there is one mainly binding site of APM, AK, TGS, SC, or REB-A in domain of BSA with relatively weak interactions. Molecular modeling results indicated that hydrogen bonding interactions were the mainly binding forces of sweeteners with BSA. Circular dichroism spectra indicated that APM and REB-A obviously induced the secondary structure changes of BSA. The presence of APM increased the fraction of α–Helix of BSA from 65.4% to 73.8%, while the presence of REB-A resulted in decreasing the fraction of α–helix of BSA from 65.4% to 51.2%. The melting temperature studies showed that these five sweeteners except REB-A act as stabilizers to increase the thermal stability of BSA during the thermal denaturation process. In addition, AK, TGS, and SC obviously increased the esterase-like activity of BSA, and such loss of activity of BSA induced by APM and REB-A.
研究领域:
生物化学
·
食品科学
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DOI
PubMed
高影响因子
ACS Applied Materials & Interfaces
·
2015
·
IF 6.723
Zhanfeng Li,Ting Yang,Chunming Lin,Quanshun Li,Songfeng Liu,Fengzhi Xu,Hongyan Wang,Xuejun Cui
A facile sonochemical approach is designed to fabricate protein nanocapsules for hydrophilic drugs (HDs), and HD-loaded multifunctional bovine serum albumin (BSA) nanocapsules (MBNCs) have been prepared for the first time. The as-synthesized HD-loaded MBNCs have a satisfying size range and an excellent magnetic responsive ability. Moreover, high-dose hydrophilic drugs could be loaded into the MBNCs. As carriers, HD-loaded MBNCs also show attractive redox-responsive controlled release ability for hydrophilic drugs and could be internalized selectively by the tumor cells through the folate-mediated endocytosis.
研究领域:
药剂学
·
生物医学工程
·
纳米医学
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DOI
PubMed
高影响因子
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
·
2026
·
IF 4.8
Xiaoqing Hao,Xiaoxuan Tan,Xinyi Feng,Jing Li,Changhu Xue
Astaxanthin-binding proteins contribute to the vibrant coloration of various organisms. Inspired by nature, artificial astaxanthin-protein systems have been developed for food applications. However, due to the structural diversity of proteins and the variable aggregation states of astaxanthin (AST) in aqueous environments, the mechanism underlying color modulation upon astaxanthin–protein binding remains poorly understood. In this study, the interactions between bovine serum albumin (BSA) and astaxanthin in either H-aggregates state (H-AST) or J-aggregates state (J-AST) were investigated using multispectral techniques and molecular dynamics (MD) simulations. H-AST/BSA and J-AST/BSA complexes were prepared using the Solvent-Induced Self-Assembly method. Meanwhile, monomer AST encapsulated BSA complex (M-AST/BSA) was prepared for comparative analysis. The stability of AST states encapsulated in BSA were characterized by ultraviolet–visible absorption spectroscopy. Fluorescence spectroscopy revealed static quenching and decreased binding affinity (M-AST > H-AST > J-AST) of AST for BSA upon the aggregation of AST. The interactions were driven by hydrophobic and electrostatic forces, dominated by both enthalpy and entropy changes. Circular dichroism (CD) showed a decrease in α-helix content and an increase in β-turn structure in BSA upon complexation. Notably, the H-AST/BSA complex underwent a transformation from H- to J-type aggregation by heating from 25 °C to 100 °C, as evidenced by MD simulations. This study provides new insights into the interaction mechanisms between astaxanthin aggregates and BSA. It also establishes a theoretical basis for understanding astaxanthin-protein-related color changes in food systems.
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PubMed
高影响因子
ACTA PHYSICO-CHIMICA SINICA
·
2016
·Vol. 32
·期 12
·2951-2960
·
IF 0.844
XIE Hu-Jun,LIU Cheng-Cheng,SUN Qiang,GU Qing,LEI Qun-Fang,FANG Wen-Jun
UV-visible (UV-Vis) absorption spectroscopy, fluorescence spectroscopy (FL), dynamic light scattering (DLS) and isothermal titration calorimetry (ITC) were used to study the interactions between bovine serum albumin (BSA) and the three quaternary ammonium surfactants N-dodecyl-N-(2-hydroxyethyl)-N,N-dimethyl
ammonium bromide (DHDAB), N-tetradecyl-N-(2-hydroxyethyl)-N,N-dimethyl ammonium bromide (THDAB) and N-cetyl-N-(2-hydroxyethyl)-N,N-dimethyl ammonium bromide (CHDAB). These surfactants quenched the intrinsic fluorescence of BSA, with longer alkyl chains
resulting in more significant quenching. This was attributed to static quenching. Further evidence of static quenching was provided by UV-Vis absorption spectroscopy. The particle size of BSA was found to initially increase and then decrease with increasing surfactant concentration. The concentration
of surfactant changed the type of interaction mode. This work revealed the mechanism and binding characteristics between surfactants and protein, and provides the basis for further applications of surfactants.
研究领域:
物理化学
·
胶体与界面科学
·
生物物理化学
·
分子生物学
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DOI
高影响因子
JOURNAL OF DISPERSION SCIENCE AND TECHNOLOGY
·
2019
·
IF 1.479
Yun Ying Zhai,Yan Bin Yun,Chun Li Li
Through precipitation polymerization approach, bovine serum albumin (BSA) molecularly imprinted polymer (MIP) was synthesized with various reagents to ascertain the optimal synthesis condition. The optimized synthesis condition is methacrylic acid (MAA) as functional monomer, N,N′-methylenebisacrylamide (MBA) as crosslinker, template molecular/functional monomer/initiator ratio of 1:6:3, and K2S2O8/NaHSO3 initiator ratio of 1:2. BSA adsorption by synthesized MIP conformed to second-order kinetic adsorption equation and Langmuir adsorption isotherm. The maximum adsorption amount of MIP was 106.2 mg/g. Moreover, when the lysozyme (LYZ) was introduced as interfering adsorbate, the separation factor was up to 3.09, indicating that the MIP has a high affinity towards BSA.
研究领域:
高分子科学
·
分析化学
·
材料科学
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DOI
高影响因子
RSC Advances
·
2018
·Vol. 8
·期 63
·35870-35877
·
IF 2.936
Guoying Su,Lin Li,Di Zhao,Bing Li,Xia Zhang
The digestion of dietary advanced glycation end products (AGEs) largely determines their absorption in humans. To help elucidate the health effects of dietary AGEs, changes in the digestive behavior of bovine serum albumin (BSA, dietary protein) caused by glycation derived from glyoxal (GO, an important precursor of AGEs) in a simulated food heating system have been investigated. The hydrothermal aggregation of BSA was suppressed by GO derived glycation, generating glycated aggregates of loose and branched structures, according to dynamic light scattering (DLS), circular dichroism (CD) spectroscopy, free sulfhydryl group, transmission electron microscopy (TEM) and small angle X-ray scattering (SAXS) results. Analysis of protein digests showed that glycation reduced the gastric and gastrointestinal digestibility of BSA and the bioavailability of all seven detected amino acids. A comparative analysis of the distribution of CML and lysine in glycated BSA digests with different molecular weights showed that carboxymethylation directly blocked the action of proteases on Lys residues.
研究领域:
食品科学
·
营养学
·
生物化学
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产品关联
DOI
PubMed
高影响因子
MACROMOLECULAR BIOSCIENCE
·
2021
·Vol. 21
·期 12
·2100269
·
IF 4.979
Chuanjin Yin,Yalu Liu,Xueju Qi,Chuanlong Guo,Xiaochen Wu
The possibility of using drug loaded bovine serum albumin (BSA) porous films as therapeutic contact lenses is investigated. Kaempferol (KAE), a hydrophobic antioxidant and anti-inflammatory agent, is incorporated into BSA porous films to form BSA/KAE films. The BSA/KAE films are transparent in the visible wavelength range of the human eye, possessing high water content and good cytocompatibility. A prolonged and sustained drug release is observed, and the in vivo efficacy of BSA/KAE films is better than the individual KAE. BSA/KAE films promoted the corneal re-epithelialization, inhibited neovascularization, and reduced the inflammation of an alkali burn induced corneal injury model. The study demonstrates the promising potential of BSA/KAE films as therapeutic contact lenses for the treatment of corneal injury, builds an available ocular drug delivery platform for ocular diseases.
研究领域:
眼科
·
药剂学
·
生物材料
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DOI
PubMed
高影响因子
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