三维有序金掺杂纳米TiO_2修饰电极用于抗肿瘤药物与DNA相互作用的研究

利用模板法在氧化铟锡(ITO)电极表面制备了三维有序多孔结构的金掺杂纳米Ti O2薄膜修饰电极(3DOM GTD/ITO),并在此修饰电极上成功固定小牛胸腺DNA(ct DNA),从而构建了一种新型的DNA生物传感器(DNA/3DOM GTD/ITO),并通过透射电镜(TEM)、扫描电镜(SEM)对修饰电极的表面形貌进行表征。采用电化学交流阻抗(EIS)法研究了ct DNA在3DOM GTD/ITO修饰电极表面的固定情况,结果表明,ct DNA已被成功地固定在3DOM GTD/ITO修饰电极表面。采用循环伏安法、微分脉冲伏安法等电化学方法研究了抗肿瘤药物槲皮素(Qu)在3DOM GTD/ITO修饰电极表面的电化学性质及与ct DNA的相互作用。结果表明,Qu在3DOM GTD/ITO修饰电极表面有1对准可逆的氧化还原峰,其氧化还原反应为2电子和2质子的转移过程。Qu可与固定在修饰电极上的ct DNA发生较强的结合作用,其结合常数(K)为3.61×106L/mol。循环伏安实验、紫外-可见吸收光谱、分子荧光光谱、圆二色性光谱均表明Qu与ct DNA之间的相互作用模式为嵌插作用。Qu与ct DNA的碱基结合具有序列选择性,对Qu与聚(d G-d C)及聚(d A-d T)的结合常数进行计算,得到结合常数比K(d G-d C)/K(d A-d T)=3.5,表明Qu与ct DNA发生嵌插作用时更倾向于结合在GC富集区域。     

电聚合茜素黄R构建辣根过氧化物酶传感器的研究

利用电聚合茜素黄R(AYR)的方法,将辣根过氧化物酶(HRP)和细胞色素c(Cyt c)固载于通过一步法电沉积的碳纳米管-金纳米粒子(MWCNTsAu NPs)复合纳米材料修饰电极表面,构筑PAYR-HRP-Cyt c/M WCNTs-Au NPs修饰电极,并利用HRP对H2O2的直接电化学催化行为对H2O2进行检测。采用扫描电镜对MWCNTs-Au NPs和PAYR-HRP-Cyt c的表面形貌进行表征。利用电化学阻抗对修饰电极的构筑过程进行了监测。采用循环伏安法和计时电流法对修饰电极的电化学行为进行了研究。探讨了p H和电位对该修饰电极测定H2O2的性能的影响。该传感器对H2O2在5.0×10-7~3.14×10-3mol/L范围内呈良好的线性响应,相关系数为0.9997,灵敏度为0.50 A·L/mol,检出限(S/N=3)为9.6×10-8mol/L。     

基于细胞色素C/氧化锌的过氧化氢生物传感器

在铟锡氧化物(ITO)导电玻璃上,通过物理气相沉积纳米氧化锌制备了Nano-ZnO/ITO,并采用浸渍法将细胞色素C(Cyt.c)直接修饰于Nano-ZnO膜上,制得了Cyt.c修饰电极(Cyt.c/Nano-ZnO/ITO/CME),构建了基于直接电子传递的过氧化氢(H2O2)生物传感器.Nano-ZnO的X射线衍射光谱表明Nano-ZnO 膜为多晶六边形纤维锌矿结构;扫描电子显微镜(SEM) 表明Nano-ZnO 膜为多孔纳米材料,微粒直径在50～100 nm,且堆积形成多孔Nano-ZnO结构;紫外可见吸收光谱的最大吸收峰为360 nm,室温禁带宽度 3.37 eV.交流阻抗、紫外可见光谱以及循环伏安法证明了吸附在Nano-ZnO上的Cyt.c保持了生物催化活性,并实现了在Nano-ZnO上的直接电子传递.H2O2生物传感器(Cyt.c/Nano-ZnO/ITO/CME)的线性范围5×10-5～5×10-3 mol/L;灵敏度7.2×10-3 A·cm-2·mol/L,检出限4×10-5mol/L; 响应时间约3 s.     

基于三维有序金掺杂纳米二氧化钛的DNA生物传感器研究

用模板法在氧化铟锡(ITO)电极上制备具有三维有序多孔结构的金掺杂纳米二氧化钛修饰电极(3DOM GTD/ITO),扫描电镜(SEM)结果表明,制备的修饰电极三维结构规整有序、孔径均一。将标记有二茂铁(Fc)的DNA探针修饰到3DOM GTD/ITO电极上构建了一种新的标记型DNA生物传感器,通过Fc在DNA探针杂交前后的电化学信号变化可识别目标靶序列。采用循环伏安(CV)、示差脉冲(DPV)和交流阻抗(EIS)等方法对DNA探针在电极表面的固定和杂交进行表征。实验结果表明,该DNA生物传感器可以成功地识别乳腺癌基因靶序列,Fc的氧化还原电流与靶序列浓度在8.0×10-7～1.0×10-5 mol/L范围内呈线性关系,线性相关系数为0.9908,检测限为5.2×10-7 mol/L。     

细胞色素c在Fe_2O_3修饰电极上的直接电化学和电催化特性

采用全氟磺酸树脂Nafion将金属氧化物Fe2O3颗粒细胞色素c(Cyt c)固定玻碳电极(GCE)表面,制备了Nafion-Cyt c-Fe2O3修饰的玻碳电极,构建了基于直接电子传递的过氧化氢生物传感器。在0.10mol/L pH7.0的磷酸盐缓冲溶液中,修饰电极的循环伏安曲线上显示出一对准可逆的氧化还原峰,式量电位为22mV。Cyt c在修饰电极表面的异相电子转移速率常数为1.21s-1。修饰后的电极对过氧化氢有良好响应,响应时间小于10s,电极的安培响应与过氧化氢浓度在2.0×10-6～3.0×10-3mol/L范围内成线性关系,检出限为1.0×10-6mol/L,米氏常数为1.35mmol/L,显示出较好的亲和力。     

磁性纳米微球-血红蛋白修饰电极的电化学行为及对H2O2电催化还原的研究

将天然高分子壳聚糖(CS)包裹碳包铁的磁性纳米微球(CFN/CS)修饰于玻碳电极表面,并利用戊二醛将血红蛋白(Hb)交联在CFN/CS上,制备了Hb-CFN/CS-GC电极。循环伏安法和电化学交流阻抗法实验结果表明,Hb在CFN/CS-GC电极表面仍保持较好的生物活性,能稳定有效地进行直接电子转移反应。电化学研究表明该修饰电极对H2O2有良好的电催化还原作用,在pH 7.0的磷酸盐(PBS)介质中,H2O2在5.2×10-5~2.3×10-3mol/L浓度范围内,其浓度与还原峰电流呈良好线性关系,检出限为8.7×10-6mol/L。该修饰电极有着良好的重现性和稳定性。     

新型金纳米材料在过氧化氢传感器中的应用

合成了新型的金纳米盒子材料,在金电极上通过金硫键自组装的方法修饰金纳米,再通过自组装和浸渍的方法修饰细胞色素c(Cyt c),构建了基于Cyt c的直接电子传递的H2O2电化学传感器,所得传感器的灵敏度为4.4A/(mol/L),线性范围为4.7×10-6~8.0×10-3 mol/L,检测限为1.5×10-6 mol/L。并将以金纳米盒子为基底的传感器与传统的电沉积金纳米,以及金纳米溶胶传感器做了对比,实验结果表明新型的金纳米盒子所修饰的传感器具有更好的灵敏度、更宽的线性范围及更低的检测限。     

细胞色素C在4,5-二氮芴-9-酮修饰玻碳电极上的直接电化学研究

采用循环伏安法探讨了细胞色素C(Cyt C)在4, 5-二氮芴-9-酮(dafo)修饰玻碳电极表面的电化学行为.结果表明,Cyt C在dafo修饰电极上呈现一对峰形较好且准可逆的氧化还原峰,其式电位(E0′)为13 mV,峰电流与扫描速度呈线性关系,该电极过程是表面控制过程,电化学反应效率常数(ks)为0.89/s.固定在dafo上的Cyt C能促进H2O2的催化还原,响应快速而灵敏(<10 s),峰电流与H2O2浓度在5.0×10-6～3.0×10-4 mol/L范围内呈线性关系;检出限2.5×10-6 mol/L;米氏常数为1.07 mmol/L,显示出较好的亲和力.     

辣根过氧化酶在磁性纳米修饰的离子注入电极上的电化学和电催化行为

辣根过氧化酶(HRP)在Co/NH2/ITO离子注入电极上有一对良好的氧化还原峰,峰电位分别为Epc=-0.2 V,Epa=-0.01 V(vsAg/AgCl)。该修饰电极对H2O2具有催化作用,可以用作H2O2的生物传感器,峰电流与H2O2的浓度分别在1.0×10-10~2.0×10-8mol/L和2.0×10-8~1.0×10-7mol/L范围内呈线性关系,线性回归方程分别为Ip(mA)=2.2986+0.06632c(nmol/L)和Ip(mA)=3.5788+7.3053E-4c(nmol/L),相关系数分别为0.9972和0.9688。检出限为1.0×10-10mol/L。     

血红蛋白在二维纳米金Langmuir—Blodgett单层膜修饰电极上的直接电化学

利用Langmuir-Blodgett(LB)技术在氧化铟锡(ITO)电极上制备了分散均匀的二维纳米金单层膜,并将血红蛋白(Hb)直接固定于该修饰电极表面,研究了Hb在电极上的直接电化学行为.实验结果表明:纳米金可以改善Hb和电极间的直接电子传递,提高电子传递效率.Hb/Nano-Au修饰电极在pH 5.0～9.0范围内的式电位与溶液pH呈线性关系,斜率为-57 mV/pH,说明Hb的电子传递过程伴随质子转移;该修饰电极对H2O2具有良好的催化作用,在0.1 mol/L pH 7.0 的磷酸盐缓冲溶液(PBS)中,H2O2在2.5×10-6～4.1×10-4 mol/L浓度范围内与响应电流呈良好的线性关系,检出限为6.2×10-7 mol/L;其异相电子转移速率常数为0.66 s-1,米氏常数为0.20 mmol/L.     

Ni(II), Pd(II), Cu(II) And Zn(II) complexes with N-(2-Pyridyl)Carbonylaniline (L), Syntheses and X-Ray Crystal structures of [Cu(L)2(H2O)2](No3)2, [Cu(L)2(H2O)2](Clo4)2 and [Zn(L)2(H2O)2](Clo4)2

Reaction of the N-(2-pyridyl)carbonylaniline ligand (L) with Cu(NO₃)₂, Cu(ClO₄)₂, Zn(ClO₄)₂, Ni(NO₃)₂ and PdCl₂ gives complexes with stoichiometry [Cu(L)₂(H₂O)₂](NO₃)₂, [Cu(L)₂(H₂O)₂](ClO₄)₂, [Zn(L)₂(H₂O)₂] (ClO₄)_2, [Ni(L)₂(H₂O)Cl](NO₃) and PdLCl₂. The new complexes were characterized by elemental analyses and infrared spectra. The crystal structures of [Cu(L)₂(H₂O)₂](NO₃)₂, [Cu(L)₂(H₂O)₂](ClO₄)₂, and [Zn(L)₂(H₂O)₂](ClO₄)₂ were determined by X-ray crystallography. The cation complexes [M(L)₂(H₂O)₂] contain copper(II) and zinc(II) with distorted octahedral geometry with two N-(2-pyridyl)carbonylaniline (L) ligands occupying the equatorial sites. The hexa-coordinated metal atoms are bonded to two pyridinic nitrogens, two carbonyl oxygens and two water molecules occupying the axial sites. Both the coordinated water molecules and uncoordinated amide NH groups of the N-(2-pyridyl)carbonylaniline (L) ligands are involved in hydrogen bonding, resulting in infinite hydrogen-bonded chains running in one and two-dimensions.     

Syntheses,characterizations and crystal structures of two new complexes, [Co2(CH2 =C(CH3)CO2)4(phen)2(H2O)2] and [Pb2(CH2 =C(CH3)CO2)4(phen)2]

Two new complexes, [Co₂(CH₂=C(CH₃)CO₂)₄(phen)₂(H₂O)₂] (1) and [Pb₂(CH₂=C(CH₃)CO₂)₄(phen)₂] (phen = 1,10-phenanthroline) (2), have been synthesized and structurally characterized by single crystal X-ray diffraction methods. There are two cocrystallized conformers of [Co(CH₂=C(CH₃)CO₂)₂(phen)(H₂O)] in the asymmetric unit of 1 with the Co atoms displaying similar coordination modes. In the asymmetric unit of 2, there exist two crystallographically independent [Pb(CH₂=C(CH₃)CO₂)₂(phen)] molecules with the Pb atoms showing completely different coordination geometries. Weak intermolecular interactions such as hydrogen bonding and π–π stacking are responsible for the supramolecular assembly and stabilization of the crystal structures of 1 and 2. The complexes are characterized by elemental analysis, IR spectra, and UV–Vis spectra. The fluorescent properties of 2 are also discussed.     

Synthesis,Characterization and Crystal Structure of （2,2′—Bipyridine）（μ—maleato）copper（Ⅱ）Dihydrate

The title polymeric complex [Cu(C₄H₂O₄)(C₁₀H₈N₂)]_n·2nH₂O was prepared and its crystal structure was determined by X‐ray diffraction methods. The crystal belongs to space group P2₁/c with cell dimensions of a = 1.0104(1), b = 1.9952(2), c = 0.7357(2) nm, β= 98.38(2)° and Z = 4. The complex forms zig‐zag chains along crystallographic axis c via Cu—O (carboxyl) bond in the apical direction. Each repeated unit consists of a square pyramidal Cu(II) centre with one maleate dianion and one 2,2′‐bipyridine forming a basal plane. Adjacent chains link to each other by H‐bonding between carboxyl groups and crystalline water. The distance of 0.3482 nm between parallel bipyridine rings shows a π‐π stacking interaction. The title complex was also characterized by IR, UV and ESR spectra.     

W(100) c(2×2)表面的STM图像

用基于第一性原理的密度泛函理论研究了W(100) c(2×2)再构表面的表面弛豫以及扫描隧道显微镜(STM)图像和衬底偏压的关系. 计算所得到的表面原子沿[-110]方向的畸变位移δ为0.027 nm, 畸变能⊿E为80.6 meV·atom-1, 表面原子的弛豫分别为-7.6%(⊿d12/d0)和+0.8%(⊿d23/d0), 功函数Φ为4.55 eV. STM图像模拟表明, 由于表面原子沿[-110]方向的位移, 会导致出现平行于[110]方向的亮暗带状条纹. STM图像中突起所对应的并不是表面或次表面的钨原子, 而是zig-zag型W 原子链中线位置; 而STM暗区对应于原子位置畸变形成的相邻zig-zag型W原子链中间区域. 当衬底负偏压时, STM针尖典型起伏高度大约在0.008-0.013 nm之间; 而当衬底正偏压时, 针尖起伏高度在0.019-0.024 nm之间变化.     

两种新型salen金属络合物WO2(salen)和MoO2-(salen)的合成

新合成了两种过渡金属salen络合物WO2(salen)和MoO2(salen).通过和已经有的文献比较,发现这两种络合物的分子结构是少见的β-cis构型.     

2-(2-Thiazolylazo)-p-cresol(TAC) as a Reagent for the Spectrophotometric Determination of Lead(II)

Abstract

The reaction between lead(II) and 2-(2-Thiazolylazo)-p-Cresol(TAC) in the presence of TERGITOL NPX (4 mg/ml) at an apparent pH 9.0–10.0 results in an intensely colored complex which is stable for at least 4 hr.

The composition of the complex is 1:2 cation: TAC and the log of the formation constant is 11.92 ± 0. 40. Beer's law is obeyed up to 6.0μg.ml^?1 of lead(II) at 650nm.

The apparent molar absorptivity at 650 nm is 2.07 × 10⁴ 1. mole^?1.cm^?1 and the detection limit was obtained as 10.0 ng.ml^?1 of lead(II).

The method is applied to determination of lead(II) in copper-base alloy.     

Comparison between Echinococcus granulosus sensu stricto (G1) and E. canadensis (G6) mitochondrial genes (cox1 and nad1) and their related protein models using experimental and bioinformatics analysis

BackgroundCystic echinococcosis (CE) as a zoonotic parasitic disease, remains a health challenge in many parts of the world. There are different species of Echinococcus granulosus sensu lato with different pathogenicity and host preferences.Different procedures have been applied for characterization of Echinococcus taxa in which two mitochondrial genes, cox1 and nad1 have been used more common. They have been able to differentiate E. granulosus sensu stricto and E. canadensis species in different hosts. The affinity of E. granulosus sensu stricto and E. canadensis species for localizing different organs seems to be different. To what such affinity and related pathogenicity could be related, is not known, so far. Bioinformatics analysis may be helpful to interpret such difference by investigating the genes and their related protein models between different species infecting human and animals. The current work was designed to study the differences between E. granulosus s.s. and E. canadensis species mitochondrial genes (cox1 and nad1) and related protein models of CE cysts by experimental and bioinformatics analysis.Materials and methodsDifferent human and animal CE cysts were collected and their DNA was extracted and sequenced based on their cox1 and nad1 genes. In order to determine the E. granulosus s.s. and E. canadensis species of the samples, BLAST analysis was performed on sequenced genes. Three sequences were selected for analysis and were deposited in GenBank. Moreover, the sequence number of KT988116.1 which belonged to E. canadensis from our already deposited in GenBank was also selected. Alignment and phylogenetic analysis were performed on the sequences using BioEdit and MEGA7 software. The raw sequences of translated proteins belonged to the mentioned genes were obtained from Protein database in NCBI. The secondary structure was determined by PSIPRED Protein Sequence Analysis Workbench. The tertiary models of COX1 and NAD1 proteins in both genotypes were constructed using Modeler 9.12 software and their physicochemical features were computed using ProtParam tool in ExPASY server.ResultsBLAST analysis on sequenced genes showed that the samples belonged to E. granulosus s.s. and E. canadensis species. These sequences were deposited in GenBank with accession numbers: JN579173.1, KF437811.1, and KY924632.1.The results showed that proteins of COX1 of E. granulosus s.s., COX1of E. canadensis, NAD1of E. granulosus s.s. and NAD1of E. canadensis species, consisted of 135, 122, 120 and 124 amino acids, respectively. The aligned sequences of translated proteins belonged to COX1 and NAD1 enzymes in E. granulosus s.s. and E. canadensis species were different; such that alignment COX1 sequence between E. granulosus s.s. and E. canadensis species showed that amino acids were different in 6 positions. This difference for NAD1 sequences were different in 19 positions. The secondary structure determined by PSIPRED showed differences in coil, strand and helix chains in COX1 and NAD1 proteins in E. granulosus s.s. and E. canadensis species. Comparison between three-dimensional structures (3D) of COX1 protein model in E. granulosus s.s. and E. canadensis species demonstrated an additional helix with two conserved iron binding sites in the COX1 protein of E. granulosus s.s. species.ConclusionE. granulosus s.s. and E. canadensis species differences are reflected in two important proteins: COX1 and NAD1. These differences are demonstrable in the 3D structure of proteins of both strains. So, the present study is adding to our understanding of the difference in molecular sequences between the E. granulosus s.s. (G1) and E. canadensis (G6) which may be used for interpreting the difference between the pathogenicity and localization affinity in these two important helminthic zoonosis.     

Syntheses and Crystal Structures of [Ni(L)_2(NCS)_2] and [Co(L)_2(NCS)_2](L=Azobis(2-pyridine)

1 INTRODUCTION The synthesis of new organic-inorganic hybrid compounds is a relatively new research area that has developed rapidly in the last several years[1]. Bische- late ligand[2, 3], such as azobis(2-pyridine), is a novel tetradentate ligand expect…     

Thetris(2-nitroso-1-naphtholato)ferrate(II) ion

Summary Thetris(2-nitroso-1-naphtholato)ferrate(II) complex is isolated in the form of its ferrous salt and characterized by analytical, infrared, and UV/Vis data. In the solid state and in solution the complex has predominantly a quinone oximic structure. The oxime group is deprotonated and bound to ironvia the nitrogen atom.

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Dastris(2-Nitroso-1-naphtholato)ferrat(II)-Ion

Zusammenfassung Dertris(2-Nitroso-1-naphtholato)ferrat(II)-Komplex wurde in der Form seines Ferrosalzes isoliert und durch Analyse und Spektroskopie (IR, UV/Vis) charakterisiert. Im festen Zustand und in Lösung hat der Komplex vorwiegend Chinonoximstruktur. Die Oximgruppe ist deprotoniert und über das Stickstoffatom an das Eisen gebunden.

     

THE INTERACTION OF 2-AMINO-2-HYDROXYMETHYL-1,3-PROPANEDIOL WITH COBALT(II) AND MANGANESE(II) IONS

Abstract

The stepwise complex formation between 2-amino-2-hydroxymethyl-1,3-propanediol (TRIS) with Co(II) and Mn(II) was studied by potentiometry at constant ionic strength 2.0 M (NaClO₄) and T = (25.0 ± 0.1)°C, from pH measurements. Data of average ligand number (Bjerrum's function) were obtained from such measurements followed by integration to obtain Leden's function, F ₀(L). Graphical treatment and matrix solution of simultaneous equations have shown two overall stability constants of mononuclear stepwise complexes for the Mn(II)/TRIS system (β₁ = (5.04 ± 0.02) M^?1 and β₂ = (5.4 ± 0.5) M^?2) and three for the Co(II)/TRIS system (β₁ = (1.67 ± 0.02) × 10² M^?1, β₂ = (7.01 ± 0.05) × 10³ M^?2 and β₃ = (2.4 ± 0.4) × 10⁴ M^?3). Slow spontaneous oxidation of Co(II) solutions by dissolved oxygen, accelerated by S(IV), occurs in a buffer solution TRIS/HTRIS⁺ 0.010/0.030 M, with a synergistic effect of Mn(II).