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Journal of Pharmaceutical Analysis · 2013 · IF 0

Investigation of the interaction between indigotin and two serum albumins by spectroscopic approaches

Zheng-Jun Cheng,Hong-Mei Zhao,Qian-Yong Xu,Rong Liu

The binding characteristics of indigotin with human serum albumin (HSA) and bovine serum albumin (BSA) have been investigated by various spectroscopic techniques. Spectroscopic analysis revealed that the quenching mechanism between indigotin and HSA/BSA belonged to the static quenching. The displacement experiments suggested that indigotin primarily bound to tryptophan residues on proteins within site I. The thermodynamic parameters indicated that the binding of indigotin–HSA/BSA mainly depended on the hydrophobic interaction. The binding distance of indigotin to HSA/BSA was evaluated. The results by synchronous fluorescence, three-dimensional fluorescence, Fourier Transform Infrared spectroscopy (FT-IR) and circular dichroism (CD) spectra showed that the conformation of proteins altered in the presence of indigotin.

CAS / MDL: 482-89-3
研究领域: 生物化学 · 药物化学 · 分子生物学
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LUMINESCENCE · 2021 ·Vol. 36 ·期 4 ·977-985 · IF 2.464

Assessment on the binding characteristics of residual marbofloxacin in animal-derived food to bovine/human serum albumin by spectroscopy and molecular modelling

Xu Li,Yue Yuan,Rui Zhao,Di Shao,Shuyun Bi

To assess the toxicity of residual marbofloxacin from animal-derived food, the interaction characteristics of marbofloxacin to bovine/human serum albumins (BSA/HSA) were explored using spectroscopic methods combined with molecular modelling. According to fluorescence spectra and time-resolved fluorescence spectra measurements, quenching of BSA/HSA fluorescence induced by marbofloxacin was characterized as static quenching. A 1:1 ground-state complex of marbofloxacin to BSA/HSA was formed with binding constant ( K a ) 1.66 × 10 4 /9.74 × 10 3 M −1 at 291 K. The location of marbofloxacin binding at site I within BSA/HSA was clarified by site marker competitive experiments. Molecular modelling demonstrated that the binding region for marbofloxacin to BSA and HSA were at site I with the lowest binding free energies of −22.86 and −21.60 kJ mol −1 , respectively. Hydrogen bonds and van der Waals forces were dominantly involved in the spontaneous binding. Nonradiation energy transferred from BSA and HSA to marbofloxacin, due to the close distance ( r 0 ) between marbofloxacin and Trp residues of BSA (4.28 nm) and HSA (3.34 nm). As explained by circular dichroism (CD) spectra, an increased BSA/HSA α- helix structure was observed after binding to marbofloxacin. Ultraviolet–visible (UV–vis) and Fourier transform infrared (FT-IR) spectra suggested that conformation of the two proteins was altered by marbofloxacin.

CAS / MDL: 115550-35-1
研究领域: 药理学 · 生物化学 · 食品安全
✓ 已验证 产品关联 DOI PubMed 高影响因子
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MOLECULAR BIOLOGY REPORTS · 2012 ·Vol. 39 ·期 10 ·9493-9508 · IF 2.929

Interaction of ergosterol with bovine serum albumin and human serum albumin by spectroscopic analysis

Cheng Zhengjun

This study was designed to examine the interactions of ergosterol with bovine serum albumin (BSA) and human serum albumin (HSA) under physiological conditions with the drug concentrations in the range of 2.99–105.88 μM and the concentration of proteins was fixed at 5.0 μM. The analysis of emission spectra quenching at different temperatures revealed that the quenching mechanism of HSA/BSA by ergosterol was the static quenching. The number of binding sites n and the binding constants K were obtained at various temperatures. The distance r between ergosterol and HSA/BSA was evaluated according to Föster non-radioactive energy transfer theory. The results of synchronous fluorescence, 3D fluorescence, FT-IR, CD and UV–Vis absorption spectra showed that the conformations of HSA/BSA altered in the presence of ergosterol. The thermodynamic parameters, free energy change (Δ G ), enthalpy change (Δ H ) and entropy change (Δ S ) for BSA–ergosterol and HSA–ergosterol systems were calculated by the van’t Hoff equation and discussed. Besides, with the aid of three site markers (for example, phenylbutazone, ibuprofen and digitoxin), we have reported that ergosterol primarily binds to the tryptophan residues of BSA/HSA within site I (subdomain II A).

CAS / MDL: 57-87-4
研究领域: 生物化学 · 药物化学
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LANGMUIR · 2016 · IF 3.993

Influence of Albumin Configuration by the Chiral Polymer-Grafted Gold Nanoparticles

Jun Deng,Zheng Li,Mengyun Yao,Changyou Gao

The interaction between nanoparticles (NPs) and proteins is a topic of high relevance for the medical application of NPs. This study reveals the molecular chirality on NP surfaces as an indirect regulator of the interaction between proteins and NPs. Poly(N-acryloyl-valine) (PAV) polymers with d- and l-configurations were conjugated onto gold NPs with a size of 5 nm to obtain the l-PAV-AuNPs and d-PAV-AuNPs, respectively. They had same chemical composition and surface grafting density but different surface chirality. The isothermal titration calorimetry results showed that adsorption of bovine serum albumin onto the l-PAV-AuNPs and d-PAV-AuNPs was primarily driven by electrostatic interaction. Dynamic light scattering, circular dichroism spectroscopy, fluorescence quenching, and isothermal titration calorimetry characterizations revealed that bovine serum albumin molecules adopted both side-on and end-on configurations on the d-PAV-AuNPs, whereas only end-on configuration on the l-PAV-AuNPs.

研究领域: 生物医学工程 · 纳米医学 · 蛋白质科学
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COLLOIDS AND SURFACES B-BIOINTERFACES · 2020 · IF 4.389

Albumin-gated zwitterion-stabilized mesoporous silica nanorod as a pH-responsive drug delivery system

Huaxin Zhang,Qinghua Xia,Dan Zhou

Silica nanoparticles as drug delivery systems (DDS) have received huge attention in nanomedicine research. However, their drug release processes were usually discussed in the absence of proteins, which are abundant in real delivery media and likely to affect the release behaviors. In this work, novel pH-sensitive silica-based DDSs were constructed using the endogenous protein, human serum albumin (HSA), as the gatekeeper, and their release properties in protein-containing media were measured for the first time. As-synthesized mesoporous silica nanorod (MSNR) was modified with zwitterions to suppress the nonspecific adsorption of protein and to improve the dispersity. HSA was fixed onto MSNR through drug-protein interactions and covalent bonds, respectively. Benzoic-imine bonds were introduced into the designs to realize pH responsiveness. The fluorescence quenching effect of drugs on HSA was used to monitor the drug release in simulated body fluids containing proteins. The results indicated that protein gating could effectively reduce premature release in normal blood environment. The endogenous protein capping, high dispersity and stability, considerable loading content, low cytotoxicity and favorable responsiveness to acidic microenvironment enable the present structures to be promising carriers for chemotherapy drugs.

研究领域: 纳米医学 · 药剂学 · 生物材料
✓ 已验证 产品关联 DOI PubMed 高影响因子
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CHEMICO-BIOLOGICAL INTERACTIONS · 2025 · IF 5.4

Antioxidant capacity and esterase activity of serum albumin toward interaction with HPPD inhibitors: Multi-spectral and computational studies

Panpan Chen,Xueqing Ding,Junqing Tu,Yi Wang

Sulcotrione and mesotrione are novel plant 4-hydroxyphenylpyruvate dioxygenase (HPPD) inhibitors. The overuse of these herbicides can bring the risk to environment and human. In this study, multispectral methods, density functional theory (DFT) calculations, and molecular docking techniques were used to investigate how sulcotrione and mesotrione interact with human serum albumin (HSA) and bovine serum albumin (BSA). The results revealed that both herbicides quenched the endogenous fluorescence of HSA/BSA through a static quenching mechanism. Circular dichroism (CD), Fourier Transform Infrared (FTIR), synchronous fluorescence, and three-dimensional (3D) fluorescence spectra demonstrated that sulcotrione and mesotrione induced conformational and secondary structural changes in HSA and BSA. Thermodynamic studies indicated that hydrogen bonding and van der Waals forces were the primary driving forces behind these interactions. Additionally, both compounds enhanced the esterase activity and antioxidant capacity of HSA and BSA while altering amino acid residues. The in vivo toxicity test and ROS levels results of zebrafish also showed that the toxicity of mesotrione was higher than that of sulcotrione. This study provides critical insights into the potential health risks posed by HPPD inhibitors to humans and mammals, emphasizing the need for further safety evaluations.

CAS / MDL: 67-68-5 69-78-3 830-03-5
研究领域: 生物化学 · 药物代谢 · 分子生物学 · 环境毒理学 · 结构生物学
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ANALYTICA CHIMICA ACTA · 2019 · IF 5.256

Online sample clean-up and enrichment of proteins from salty media with dynamic double gradients on a paper fluidic channel

Yu Cai,Ji-Cheng Niu,Yu-Qi Liu,Xin-Li Du,Zhi-Yong Wu

Paper-based analytical device (PAD) has received more and more attention in the field of point-of-care test (POCT) due to its low cost, portability and simple operation. Sensitivity and selectivity are two important aspects in clinical diagnostic analysis. However, low sensitivity of a PAD limits its wider application for POCT. Here we introduced a PAD that can clean and enrich the protein content from salty media with both electric field (E) and pH gradient (double E/pH gradients), with which 100-fold enrichment effect could be achieved within 70 s as demonstrated by fluorescein isothiocyanate labeled bovine serum albumin (FITC-BSA) from artificial urine media. With post staining of the protein stacking band with bromophenol blue (BPB), selective colorimetric detection of human serum albumin (HSA) was achieved simply with smartphone camera in the clinically significant range of 10–300 mg‧L −1 (R 2  = 0.99) with a limit of detection (LOD) of 4.9 mg‧L −1 . Detection of microalbuminuria (MAU) of diabetic patients was demonstrated with this method without difference (ɑ = 0.01) to that by the clinical method (immunoturbidimetry). This work demonstrated the potential of this PAD method in online sample pretreatment and detection of target component from complex physiological samples.

研究领域: 分析化学 · 生物医学工程 · 临床诊断
✓ 已验证 产品关联 DOI PubMed 高影响因子
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FOOD RESEARCH INTERNATIONAL · 2024 · IF 7

The mechanism of resveratrol stabilization and degradation by synergistic interactions between constituent proteins of whey protein

Xin Yin,Wusigale,Hao Cheng,Paul Van der Meeren,Li Liang

Whey protein isolate (WPI) is mainly composed of β-lactoglobulin (β-LG), α-lactalbumin (α-LA) and bovine serum albumin (BSA). The aim of this study was to compare and analyze the influence of WPI and its three main constituent proteins, as well as proportionally reconstituted WPI (R-WPI) on resveratrol. It was found that the storage stability of resveratrol was protected by WPI, not affected by R-WPI, but reduced by individual whey proteins at 45°C for 30 days. The rank of accelerated degradation of resveratrol by individual whey proteins was BSA > α-LA > β-LG. The antioxidant activity, localization of resveratrol and oxidation of carrier proteins were determined by ABTS, H 2 O 2 assay, synchronous fluorescence, carbonyl and circular dichroism. The non-covalent interactions and disulfide bonds between constituent proteins improved the antioxidant activity of the R-WPI-resveratrol complex, the oxidation stability of the carrier and the solvent shielding effect on resveratrol, which synergistically inhibited the degradation of resveratrol in R-WPI system. The results gave insight into elucidating the interaction mechanism of resveratrol with protein carriers.

CAS / MDL: 28752-68-3
研究领域: 食品科学 · 生物化学
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MOLECULES · 2023 ·Vol. 28 ·期 2 ·880 · IF 4.6

Research and Application of Kupffer Cell Thresholds for BSA Nanoparticles

Huanhuan Guo,Zongguang Tai,Fang Liu,Jing Tian,Nan Ding,Zhongjian Chen,Shen Gao

Over the past decade, the dose of nanoparticles given to solid tumors has remained at a median of 0.7% of the injected dose. Most nanoparticles are trapped in a mononuclear phagocyte system (MPS), of which 85% are Kupffer cells. In our study, threshold doses of bovine serum albumin (BSA) nanoparticles were investigated for the uptake of Kupffer cells in vitro and in vivo. The antitumor effect and safety of albumin-bound paclitaxel (ABP) were improved by using threshold doses of BSA nanoparticles. We found a threshold dose of 20,000 nanoparticles per macrophage uptake in vitro and a saturation dose of 0.3 trillion nanoparticles in tumor-bearing mice. In vivo efficacy and safety evaluations demonstrated that the threshold doses of blank BSA nanoparticles could significantly improve the efficacy and safety of ABP against tumors compared with ABP alone. In this study, the delivery efficiency of ABP was improved by using blank nanoparticles to saturate Kupffer cells, which provided a new approach to studying the Kupffer cell saturation threshold and thus a new scheme for improving the curative effect of ABP.Keywords:nanoparticles;drug delivery;breast cancer;Kupffer cell;albumin-bound paclitaxel (ABP);bovine serum albumin (BSA)

CAS / MDL: 64-17-5
研究领域: 药理学 · 肿瘤学 · 纳米技术
✓ 已验证 产品关联 DOI PubMed 高影响因子
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Journal of Advanced Research · 2020 · IF 6.992

Half-life determination of inorganic-organic hybrid nanomaterials in mice using laser-induced breakdown spectroscopy

Yanwu Chu,Zhanjie Zhang,Qianyuan He,Feng Chen,Ziqian Sheng,Deng Zhang,Honglin Jin,Fagang Jiang,Lianbo Guo

Inorganic or inorganic-organic hybrid nanomaterials have great potential for applications in the biomedical fields. Biological half-life is an essential pharmacokinetic parameter for these materials to function in vivo . Compared to inductively coupled plasma mass spectrometry (ICP-MS), which is the gold standard, laser-induced breakdown spectroscopy (LIBS) is a faster and more efficient elemental detection method. We investigated an efficient way to quantify the metabolic rate using LIBS. Nanoparticle platforms, such as manganese dioxide-bovine serum albumin (MnO 2 -BSA) or boehmite-bovine serum albumin (AlO(OH)-BSA) were injected into mice through intravenous administration for LIBS spectrum acquisition. First, the spectral background was corrected using the polynomial fitting method; The spectral interference was eliminated by Lorentz fitting for each LIBS spectrum simultaneously. The support vector regression (SVR) was then used for LIBS quantitative analyses. Finally, the LIBS results were compared with the ICP-MS ones. The half-lives of MnO 2 -BSA calculated by LIBS and ICP-MS were 2.49 and 2.42 h, respectively. For AlO(OH)-BSA, the half-lives detected by LIBS and ICP-MS were 3.46 and 3.57 h, respectively. The relative error of LIBS is within 5% compared to ICP-MS. The results demonstrate that LIBS is a valuable tool for quantifying the metabolic rates with a high degree of accuracy.

研究领域: 生物医学工程 · 分析化学 · 药代动力学
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ACS Omega · 2023 · IF 4.1

Multilayer Heterogeneous Membrane Biosensor Based on Multiphysical Field Coupling for Human Serum Albumin Detection

Haoyu Wang,Pengli Xiao,Shengbo Sang,Honglie Chen,Xiushan Dong,Yang Ge,Xing Guo,Dong Zhao

A factor closely associated with renal disease status in clinical diagnosis is abnormal human serum albumin (HSA) concentration levels in human body fluids urine, serum, etc. The surface stress biosensor was developed as a new type of biosensor to detect protein molecule concentration and has a wide range of clinical applications. However, further sensitivity improvement is required to achieve higher detection performance. Herein, MXene/PDMS/Fe3O4/PDMS of the multilayer heterogeneous membrane biosensor (MHBios) based on the coupling of the magnetic field, electric field, and surface stress field was successfully developed to achieve high sensitivity HSA detection through magnetic sensitization. The modified antibody specifically binds to HSA at the AuNP layer, allowing the biosensor to convert the surface stress caused by PDMS film deformation into an electrical signal. When the biosensor was exposed to a uniform magnetic field, the conductive path of the conductive layer was reshaped further as the magnetic force amplified the deformation of the PDMS film, enhancing the conversion of biological signals to electrical signals. The results exhibited that the detection limit (LOD) of the MHBios was 78 ng/mL when HSA concentration was 0–50 μg/mL, which was markedly lower than the minimum diagnostic limit of microalbuminuria. Furthermore, the MHBios detected HSA in actual samples, confirming the potential for early disease screening.

研究领域: 生物医学工程 · 材料科学 · 传感器与执行器 · 医疗诊断
✓ 已验证 DOI PubMed 高影响因子
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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES · 2024 · IF 7.7

Albumin as a functional carrier solubilizing and facilitating fusidic acid transmembrane delivery into Gram-negative bacteria

Xueer Zhou,Meng Wang,Yue Wang,Jianhong Liu,Chaoliang Zhang,Jian Pan,Qiang Peng

Reversing the bacterial resistance is of great significance and importance. Fusidic acid (FA) is commonly effective against Gram-positive bacterial infections, but most Gram-negative bacteria have intrinsic resistance to FA, primarily due to the strong cell membrane-FA interactions, which highly inhibit the intracellular transport of FA. Herein, we use albumin (bovine serum albumin, BSA) as a bifunctional carrier to solubilize FA and facilitate its transmembrane delivery into Gram-negative bacterial cells. The water solubility of FA is significantly enhanced from 11.87 to 442.20 μg/mL by 5 mg/mL BSA after forming FA-BSA complex. Furthermore, FA-BSA (200 μg/mL) causes 99.96 % viability loss to the model pathogen E. coli upon incubation for 3 h, while free FA or BSA alone shows little activity. Elongation of E. coli cells after treated by FA-BSA is demonstrated by SEM, and the transmembrane transport of FA-BSA is demonstrated by CLSM. Interestingly, increasing the BSA amount substantially reduce the antibacterial activity of FA-BSA, implying an albumin-based transmembrane delivery mechanism may exist. This is the first report regarding successfully reversing the intrinsic resistance of Gram-negative bacteria to FA in the form of FA-BSA. The ready availability of albumin and the simple preparation allows FA-BSA to have great potentials for clinical use.

CAS / MDL: 6990-06-3
研究领域: 微生物学 · 药学 · 生物技术
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