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High sensitivity detection of baicalein by N,S co⁃doped carbon dots and their application in biofluids
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作者 FAN Junmei LIU Wei +5 位作者 ZHU Ruitao QIN Chenxi LEI Xiaoling WANG Haotian WANG Jiao HAN Hongfei 《无机化学学报》 SCIE CAS CSCD 北大核心 2024年第10期2009-2020,共12页
In this work,p⁃phenylenediamine and L⁃cysteine were used as raw materials,and water⁃soluble N,S co⁃doped carbon dots(N,S⁃CDs)with excellent performance were prepared through a one⁃step solvothermal method.The morpholo... In this work,p⁃phenylenediamine and L⁃cysteine were used as raw materials,and water⁃soluble N,S co⁃doped carbon dots(N,S⁃CDs)with excellent performance were prepared through a one⁃step solvothermal method.The morphology and structure of N,S⁃CDs were characterized by transmission electron microscope,X⁃ray diffrac⁃tion,Fourier transform infrared spectroscopy,and X⁃ray photoelectron spectroscopy,and the basic photophysical properties were investigated via UV⁃Vis absorption spectra and fluorescence spectra.Meanwhile,the N,S⁃CDs have excellent luminescence stability with pH,ionic strength,radiation time,and storage time.Experimental results illus⁃trated the present sensor platform exhibited high sensitivity and selectivity in response to baicalein with a detection limit of 85 nmol·L-1.The quenching mechanism is proved to be the inner filter effect.In addition,this sensor can also detect baicalein in biofluids(serum and urine)with good accuracy and reproducibility. 展开更多
关键词 N S⁃carbon dots solvothermal method BAICALEIN fluorescent sensor
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氯乙酸生产工艺及改造方案 被引量:1
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作者 陈建强 王国栋 杨彩霞 《氯碱工业》 CAS 2013年第11期37-38,共2页
介绍间歇硫黄法、醋酐法及连续氯化法的氯乙酸生产工艺,分析了济宁金威煤电有限公司间歇硫黄法生产工艺的优缺点,并对存在的问题提出了改造方案。
关键词 氯乙酸 乙酸 氯化反应 硫黄法 醋酐法 连续氯化法
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Exploring the binding mechanism of thioflavin-T to the β-amyloid peptide by blind docking method 被引量:3
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作者 ZHAO DeSheng CHEN YongXiang +2 位作者 LIU Qian ZHAO YuFen LI YanMei 《Science China Chemistry》 SCIE EI CAS 2012年第1期112-117,共6页
Using blind dock method,we find that thioflavin-T(ThT) can bind to both monomers and fibrils of the full-length β-amyloid peptide(Aβ1-42) and has a higher binding affinity to the fibrils.It is shown that the hydroph... Using blind dock method,we find that thioflavin-T(ThT) can bind to both monomers and fibrils of the full-length β-amyloid peptide(Aβ1-42) and has a higher binding affinity to the fibrils.It is shown that the hydrophobic interaction between the ligand(ThT) and substrate(Aβ1-42) are stronger than hydrogen bonds.Furthermore,ThT tends to be located near the C-terminus of Aβ monomer through hydrophobic and electrostatic interactions,while it tends to contact the residues Met35 and Gly27 of the fibril surface mainly through hydrophobic interaction.Finally,according to the docking results and ThT fluorescence assay,a kinetic equation is proposed to deduce the aggregation rate coefficient of Aβ1-42. 展开更多
关键词 THT AΒ1-42 AUTODOCK aggregation kinetic equation
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