JOURNAL OF CHEMICAL TECHNOLOGY AND BIOTECHNOLOGY
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2020
·Vol. 95
·期 8
·2195-2207
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IF 2.75
Wei Shi,Si-Qi Zhang,Kai-Bin Li,Ye-Jing Deng,Chen-Yi Wang,Yi-Ting Lu,Jiao-Jiao Liu,De-Man Han
BACKGROUND Hydrophobic interaction chromatography (HIC), as a typical separation technology, often suffers from low selectivity because it has a single interaction mode. Herein, a novel HIC resin (Octyl@BSA) with imprinted layer was synthesized and used for protein adsorption. Bovine serum albumin (BSA) and bovine serum γ-globulin (bIgG) were used as model competitive proteins in this study. The effects of pH, salt type, concentration, and mass ratio were then investigated. RESULTS The data from the static and dynamic adsorption experiments indicated that the introduction of spatial recognition effectively reduced the adsorption of competitive proteins, leading to significant improvements in selectivity. In comparison with raw HIC resin, Octyl@BSA retained a high binding capacity for BSA but rejected other proteins through spatial recognition. The maximum selectivity factors ( α ) of this resin may be close to 5. The adsorption kinetics and frontal adsorption experiments further confirmed the improvement in selectivity in batch and column mode. In addition, the recyclability of Octyl@BSA was tested using ten continuous BSA adsorption–desorption cycles. CONCLUSION This study demonstrated that the introduction of spatial recognition was an effective strategy for enhancing the advantage of target proteins during competitive adsorption, leading to an improvement in selectivity for HIC. © 2020 Society of Chemical Industry
研究领域:
生物化学
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分离技术
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DOI
高影响因子
JOURNAL OF CHROMATOGRAPHY A
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2014
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IF 4.258
Chusheng Liu,Weijia Chen,Guangxin Yuan,Yao Xiao,Jacques Crommen,Shihai Xu,Zhengjin Jiang
In order to investigate the effects of the crosslinker on the separation performance of polar zwitterionic sulfoalkylbetaine-type monolithic columns, three crosslinkers, i.e. 1,4-bis(acryloyl)piperazine (PDA), ethylene dimethacrylate (EDMA) and N , N ′-methylenebisacrylamide (MBA), were copolymerized with the hydrophilic monomer N , N -dimethyl- N -acryloyloxyethyl- N -(3-sulfopropyl)ammonium betaine (SPDA). The chromatographic properties of the three hydrophilic sulfoalkylbetaine-type monolithic columns, including column efficiency, permeability, porosity and separation mechanism, were systematically compared using scanning electron microscopy or micro-HPLC. Good selectivity in micro-HPLC separations was achieved on all three monolithic columns. The results indicate that the polarity of sulfoalkylbetaine-type monolithic columns may be related to the polarity of the crosslinker, which further affects column selectivity and efficiency. A particularly high column efficiency (100,000 plates/m) was obtained on the novel poly(SPDA- co -PDA) monolithic column at a linear velocity of 1 mm/s using thiourea as test analyte. A higher resolution was also observed for nucleobases, nucleosides and hydrophilic organic acids on this novel poly(SPDA- co -PDA) monolithic column compared to the other two columns.
研究领域:
分析化学
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色谱技术
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DOI
PubMed
高影响因子
INDUSTRIAL & ENGINEERING CHEMISTRY RESEARCH
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2018
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IF 3.141
Pan Sun,Kun Huang,Jieyuan Lin,Huizhou Liu
PEG-based aqueous two-phase systems (ATPS) for extraction and removal of metal ions from industrial wastewaters is a promising strategy to replace traditional organic-aqueous two phase systems, due to its environmentally friendly advantages and excellent separation efficiency from controllable phase structure and physicochemical properties. However, controversy still remains about the partitioning mechanism of metal ions into the PEG-rich phase in ATPS. The present contribution revealed that a specific hydrophobic interaction was a main driving force for the transferring of Cr(VI) ions into the PEG-rich phase in ATPS. The properties of aqueous media around the PEG molecules and Cr(VI) ions also played a crucial role in the partitioning of Cr(VI) ions in the PEG-base ATPS. The PEG-rich phase in the ATPS exhibited a specific affinity toward poorly hydrated HCrO4– ions, compared to the strongly hydrated CrO42– ions. The difference in the properties of aqueous media in the coexisting liquid phases was response for the partitioning of Cr(VI) ions in the PEG-base ATPS. It was confirmed by combined application of UV–vis spectroscopy and molecular dynamics simulations. The present work provides a new understanding into the microscopic mechanism of the partitioning of metal ions in the polymer-based ATPS.
研究领域:
环境科学
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化学
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DOI
高影响因子
Materials
·
2015
·Vol. 8
·期 12
·8701-8713
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IF 2.651
Kaikai Wang,Juan Wang,Wenwen Hu,Yifan Zhang,Feng Zhi,Zaigang Zhou,Jinhui Wu,Yiqiao Hu
Hemoglobin is a promising drug carrier but lacks extensive investigation. The chemical conjugation of hemoglobin and drugs is costly and complex, so we have developed curcumin-loaded hemoglobin nanoparticles (CCM-Hb-NPs) via self-assembly for the first time. Using the acid-denaturing method, we avoid introducing denaturants and organic solvents. The nanoparticles are stable with uniform size. We have conducted a series of experiments to examine the interaction of hemoglobin and CCM, including hydrophobic characterization, SDS-PAGE. These experiments substantiate that this self-assembly process is mainly driven by hydrophobic forces. Our nanoparticles achieve much higher cell uptake efficiency and cytotoxicity than free CCM solutionin vitro. The uptake inhibition experiments also demonstrate that our nanoparticles were incorporated via the classic clathrin-mediated endocytosis pathway. These results indicate that hemoglobin nanoparticles formed by self-assembly are a promising drug delivery system for cancer therapy.Keywords:drug carrier;hydrophobic forces;self-assemble;cell uptake
研究领域:
生物化学
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药剂学
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肿瘤学
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产品关联
DOI
PubMed
高影响因子
JOURNAL OF MOLECULAR STRUCTURE
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2015
·
IF 1.602
Yan-Qing Wang,Hong-Mei Zhang,Yi-Jun Kang,Yun-Lan Gu,Jian Cao
In the present study, the experimental and theoretical methods were used to analyze the binding interaction of food dye , curcumin with trypsin. The results of fluorescence spectroscopic measurements indicated that curcumin binding resulted in the obviously intrinsic fluorescence quenching with the increase concentration of curcumin. This binding interaction is a spontaneous process with the estimated enthalpy and entropy changes being −15.70 kJ mol −1 and 40.25 J mol −1 K −1 , respectively. Hydrogen bonds and hydrophobic forces played an important role in the complex formation between curcumin and trypsin. Moreover, curcumin could enter into the primary substrate-binding pocket and makes the activity of trypsin decrease remarkably with the increasing concentration of curcumin.
研究领域:
生物化学
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分子生物学
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药物化学
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DOI
高影响因子
FOOD HYDROCOLLOIDS
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2024
·
IF 11
Hanyu Li,Minghui Zhao,Jinghong Li,Jiaqi Wang,Huajiang Zhang,Jing Wang,Ning Xia,Zhongjiang Wang,Ahmed M. Rayan
The pH-driven method, recognized for its material safety and avoidance of organic solvents, is considered a promising approach for the encapsulation of hydrophobic active substances. However, the interaction mode and mechanism between carriers and receptors in two stages (alkalization and neutralization) remain underexplored. In this study, the hydrophilic globular protein ovalbumin (OVA) was utilized as a carrier to load curcumin (Cur) by the pH-driven method, with an alkalization pH of 8–12. The results indicated that the solubility of Cur and the degree of protein unfolding increased with increasing alkalization pH, with a transformation in the secondary structure observed at pH 12. During the alkalization stage at pH 11 and 12, the loading efficiency of Cur exceeded 90%, with binding constants reaching as high as 5.79 × 10 5 M −1 and 1.44 × 10 5 M −1 , respectively. The interactions transitioned through three phases in the alkalization process: electrostatic dominance to hydrophobic dominance, electrostatic assistance to hydrophobic dominance, and electrostatic repulsion hindrance. Notably, the generation of electrostatic repulsion and the potential loss of binding sites resulted in a decrease in the binding affinity between OVA and Cur at pH 12. In the neutralization stage, a stable structure dominated by hydrogen bonds and van der Waals forces was observed, with Cur encapsulated within the hydrophobic core of OVA. The mechanism proposed in this study elucidates the factors affecting the efficacy of the pH-driven method and helps to refine the application in hydrophobic active substance delivery systems.
研究领域:
食品科学
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生物化学
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药物递送系统
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DOI
高影响因子
MACROMOLECULAR RAPID COMMUNICATIONS
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2025
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IF 4.3
Luyao Xing,Jiaqiang Ding,Jiaqi Gao,Dongliang Chen,Chengdong Xiong,Zuochun Xiong
The self-assembly of macromolecular segments promotes the fabrication of polymer microspheres with multiple morphologies. Inspired by the xanthium shells, A dual-driven self-assembly method have defined that enables the construction of multi-dimensional morphologies on the microsphere surface at emulsion-confined interfaces. The two driving forces are derived from the phase separation caused by the immiscibility of macromolecular segments and the different interactions between chain segments of different hydrophilicity and water molecules. The synergistic effects of these two forces, the xanthium shell structure is constructed on the microsphere surface, enabling the development of increasingly complex superstructure. This scalable approach provides extensive potential for the self-assembly technology of block copolymers with opposite properties.
研究领域:
材料科学
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高分子化学
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仿生学
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DOI
PubMed
高影响因子
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
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2015
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IF 2.858
Ming Ying,Fengwen Huang,Haidong Ye,Hong Xu,Liangliang Shen,Tianwen Huan,Shitong Huang,Jiangfeng Xie,Shengli Tian,Zhangli Hu,Zhendan He,Jun Lu,Kai Zhou
The interaction between curcumin and pepsin was investigated by fluorescence, synchronous fluorescence, UV–vis absorption, circular dichroism (CD), and molecular docking. Under physiological pH value in stomach, the fluorescence of pepsin can be quenched effectively by curcumin via a combined quenching process. Binding constant ( K a ) and binding site number ( n ) of curcumin to pepsin were obtained. According to the theory of Förster's non-radiation energy transfer, the distance r between pepsin and curcumin was found to be 2.45 nm within the curcumin–pepsin complex, which implies that the energy transfer occurs between curcumin and pepsin, leading to the quenching of pepsin fluorescence. Fluorescence experiments also suggest that curcumin is located more closely to tryptophan residues than tyrosine residues. CD spectra together with UV–vis absorbance studies show that binding of curcumin to pepsin results in the extension of peptide strands of pepsin with loss of some β-sheet structures. Thermodynamic parameters calculated from the binding constants at different temperatures reveal that hydrophobic force plays a major role in stabilizing the curcumin–pepsin complex. In addition, docking results support the above experimental findings and suggest the possible hydrogen bonds of curcumin with Thr-77, Thr-218, and Glu-287 of pepsin, which help further stabilize the curcumin–pepsin complex.
研究领域:
生物化学
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药物化学
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分子生物学
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产品关联
DOI
PubMed
高影响因子
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
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2013
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IF 1.977
Hua Li,Juanjuan Pu,Yi Wang,Chuang Liu,Jie Yu,Tao Li,Ruiqiang Wang
The interactions between Trypsin and bifendate (DDB) or analogs (I, II and III) were investigated by fluorescence, UV–visible absorption, resonance light scattering, synchronous fluorescence and 3D spectroscopy under mimic physiological conditions. The results revealed that DDB and analogs caused the fluorescence quenching of Trypsin by the formation of DDB/I/II/III–Trypsin complex. The quenching and energy transfer mechanisms were discussed. The binding constants and thermodynamic parameters at three different temperatures were obtained. The hydrophobic interaction was the predominant intermolecular forces to stabilize the complex. Results showed that DDB was the stronger quencher and bound to Trypsin with higher affinity than other three analogs.
研究领域:
生物化学
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药物化学
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分子生物学
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产品关联
DOI
PubMed
高影响因子
APPLIED SPECTROSCOPY
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2013
·
IF 1.942
Yunchang Fan,Sheli Zhang,Qiang Wang,Junhai Li,Haotian Fan,Dongkai Shan
The molecular mechanism of the interaction between pepsin and two typical ionic liquids (ILs), 1-butyl-3-methylimidazolium chloride ([C4mim]Cl) and 1-octyl-3-methylimidazolium chloride ([C8mim]Cl), was investigated with fluorescence spectroscopy, ultraviolet absorption, and circular dichroism spectroscopy at a pH value of 1.6. The results suggest that ILs could quench the intrinsic fluorescence of pepsin, probably via a dynamic quenching mechanism. The fluorescence quenching constants were determined by employing the classic Stern-Volmer equation. The constant values are very small, indicating that only a very weak interaction between ILs and pepsin exists. The Gibbs free-energy change, enthalpy change (ΔH), and entropy change (ΔS) during the interaction of pepsin and ILs were estimated. Positive values of ΔH and ΔS indicate that the interaction between ILs and pepsin is mainly driven by hydrophobic interaction. Synchronous and three-dimensional fluorescence spectra demonstrate that the addition of ILs (0–0.20 mol L−1 for each IL) does not bring apparent changes to the microenvironments of tyrosine and tryptophan residues. Activity experiments show that the activity of pepsin is concentration dependent; higher concentrations of ILs (>0.22 mol L−1 for [C8mim]Cl and >0.30 mol L−1 for [C4mim]Cl) cause the remarkable reduction of enzyme activity. The presence of ILs also does not improve the thermal stability of pepsin.
研究领域:
生物化学
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分子生物学
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DOI
PubMed
高影响因子
JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY
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2014
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IF 2.803
Yan-Qing Wang,Hong-Mei Zhang,Jian Cao,Bo-Ping Tang
Interactions of bisphenol S, a new bisphenol analogue with bovine serum albumin and calf thymus DNA were investigated using different spectroscopic methods and molecular modeling calculation. According to the analysis of experimental and theoretical data, we concluded that hydrophobic interactions and hydrogen bonding primarily mediated the binding processes of bisphenol S with bovine serum albumin and DNA. In addition, the electrostatic force should not be excluded. Molecular modeling studies indicated that the binding site of bisphenol S to bovine serum albumin located in the subdomain IB, while bisphenol S was a groove binder of DNA. In addition, BPS did not obviously induce second structural changes of bovine serum albumin, but it induced a conformational change of calf thymus DNA.
研究领域:
生物化学
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分子生物学
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DOI
高影响因子
Food Science and Technology
·
2023
·
IF 2.602
LI Gang,GE Xiaohong
Icariin has low bioavailability and poor stability, which limits its wide application. The complexation of icariin and whey protein is expected to solve this problem, but there is no research on their interaction mechanism. In view of this, the related mechanism was studied systematically by spectrofluorimetry and molecular docking method in this study. The fluorescence analysis showed that icariin and whey protein could form a non-covalent complex driven by hydrophobic force, which led to the fluorescence quenching of whey protein. In this process, the microenvironment around the tyrosine residue and tryptophan residue of whey protein changed. The molecular docking analysis confirmed the existence of hydrophobic interaction and hydrogen bonding in the complex, which well confirmed fluorescence results. The obtained results can promote the application of icariin in food.
研究领域:
食品科学
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生物化学
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产品关联
DOI
高影响因子