黄酮类药物与氯金酸的作用及其分析应用

将4种黄酮类药物染料木素、木犀草素、大豆素及柚皮素与氯金酸在不同酸度条件下反应形成金纳米颗粒. 研究发现, 生成的金纳米颗粒的等离子体共振吸收信号与4种黄酮类药物的浓度呈线性关系, 从而建立了这4种典型黄酮类药物的测定方法. 分析了黄酮类药物的分子结构并利用Materials-studio 4.0软件计算了各原子的电子云密度分布. 结果表明, 4种黄酮类药物与氯金酸作用的适宜酸度与黄酮类化合物结构中的酚羟基数和碱性氧的电子云密度分布有关.     

Optimization of high-yield biological synthesis of single-crystalline gold nanoplates

In this work, single-crystalline gold nanoplates were obtained by reducing aqueous chloroauric acid solution with the extract of Sargassum sp. (brown seaweed) at room temperature. The gold nanoplates so obtained were characterized by UV-vis spectroscopy, X-ray diffraction, atomic force microscopy, and transmission electron microscopy. The formation of gold nanoplates was found to depend on a number of environmental factors, such as the time taken to age the seaweed extract, pH of the reaction medium, reaction temperature, reaction time, and initial reactant concentrations. The size of the gold nanoplates could be controlled to between 200 and 800 nm by manipulating the initial reactant concentrations. The yield of the flat gold nanocrystals relative to the total number of nanoparticles formed was as high as approximately 80-90%.     

Specific covalent immobilization of proteins through dityrosine cross-links

Dityrosine cross-links are widely observed in nature in structural proteins such as elastin and silk. Natural oxidative cross-linking between tyrosine residues is catalyzed by a diverse group of metalloenzymes. Dityrosine formation is also catalyzed in vitro by metal-peptide complexes such as Gly-Gly-His-Ni(II). On the basis of these observations, a system was developed to specifically and covalently surface immobilize proteins through dityrosine cross-links. Methacrylate monomers of the catalytic peptide Gly-Gly-His-Tyr-OH (GGHY) and the Ni(II)-chelating group nitrilotriacetic acid (NTA) were copolymerized with acrylamide into microbeads. Green fluorescent protein (GFP), as a model protein, was genetically tagged with a tyrosine-modified His6 peptide on its carboxy terminus. GFP-YGH6, specifically associated with the NTA-Ni(II) groups, was covalently coupled to the bead surface through dityrosine bond formation catalyzed by the colocalized GGHY-Ni(II) complex. After extensive washing with EDTA to disrupt metal coordination bonds, we observed that up to 75% of the initially bound GFP-YGH6 remained covalently bound to the bead while retaining its structure and activity. Dityrosine cross-linking was confirmed by quenching the reaction with free tyrosine. The method may find particular utility in the construction and optimization of protein microarrays.     

金纳米粒子的阳光光化学合成和晶种媒介生长

在柠檬酸盐-HAuCl4溶液体系中, 于高原太阳紫外线辐射下光化学合成了分散良好、尺寸分布窄的胶体金纳米粒子. 研究了溶液的酸度和太阳辐射条件对Au(Ⅲ)离子光化学还原反应速率和形成金纳米粒子尺寸的影响; 采用晶种媒介生长技术, 通过改变Au(0)/Au(Ⅲ)比合成了平均直径为4.9~9.7 nm的球形金粒子. 根据紫外-可见吸收光谱和透射电子显微镜的表征和分析, 讨论了光化学反应中自由基反应、金纳米粒子成核和生长机理.     

Structural control of peptide-coated gold nanoparticle assemblies by the conformational transition of surface peptides

Gold nanoparticles having peptide chains on the surfaces have been prepared yb ring-opening polymerization of gamma-methyl L-glutamate N-carboxyanhydride with fixed amino groups on the nanoparticle surface as an initiator. The number of peptide chains on the surface was adjusted to ca. 2 molecules per gold nanoparticle by controlling the number of fixed amino groups on the surface. The peptide chains on the surface were partially saponified to obtain poly(gamma-methyl L-glutamate-co-L-glutamic acid) with 28 mol% of glutamic acid residues. The number-average molecular weight of the peptide was 73,000. We described structural control of the peptide-coated gold nanoparticle assembly by conformational transition of the surface peptides. In deionized water, the peptide chains on the nanoparticle took a random coil conformation, and the individual nanoparticles existed in dispersed globular species. On the other hand, the peptide chains on the nanoparticle took an alpha-helical conformation in trifluoroethanol. Under this condition, the alpha-helical peptide chains on distinct gold nanoparticles connected the nanoparticles to form a fibril assembly owing to the dipole-dipole interaction between the surface peptide chains. The morphology of the peptide-coated gold nanoparticle assembly could be controlled by the conformational transition of surface peptides, which was attended by solution composition changes.     

Electron Transfer in Peptides: On the Formation of Silver Nanoparticles

Some microorganisms perform anaerobic mineral respiration by reducing metal ions to metal nanoparticles, using peptide aggregates as medium for electron transfer (ET). Such a reaction type is investigated here with model peptides and silver as the metal. Surprisingly, Ag⁺ ions bound by peptides with histidine as the Ag⁺‐binding amino acid and tyrosine as photoinducible electron donor cannot be reduced to Ag nanoparticles (AgNPs) under ET conditions because the peptide prevents the aggregation of Ag atoms to form AgNPs. Only in the presence of chloride ions, which generate AgCl microcrystals in the peptide matrix, does the synthesis of AgNPs occur. The reaction starts with the formation of 100 nm Ag@AgCl/peptide nanocomposites which are cleaved into 15 nm AgNPs. This defined transformation from large nanoparticles into small ones is in contrast to the usually observed Ostwald ripening processes and can be followed in detail by studying time‐resolved UV/Vis spectra which exhibit an isosbestic point.     

Stable polydiacetylene/ZnO nanocomposites with two-steps reversible and irreversible thermochromism: the influence of strong surface anchoring

The influence of pH value on gold nanoparticle production in the presence of Pluronic stabilizers is systematically investigated. The reactions are studied as a function of pH and at fixed concentrations of the two reactants, HAuCl(4) and P123 block copolymer. Results indicate that the reaction pathway during the nanoparticle formation can be controlled by varying pH. The nanoparticles synthesized at pH=11.12 have an average diameter of 9.6 nm with a narrow size distribution, and the Pluronics are adsorbed on individual gold particle surfaces to form core-shell structures via hydrophobic interactions. The present work provides an economic way to improve the dispersion and stabilization of gold nanoparticles and throws further light on the understanding of gold nanoparticle production using block copolymers.     

Electrochemical nucleation of gold nanoparticles in a polymer film at a liquid-liquid interface

Simultaneous nucleation of gold nanoparticles and polymerization of tyramine has been carried out at an immiscible electrolyte interface. By transferring the gold ion of tetraoctylammoniumtetracloroaurate (TOAAuCl(4)) from the organic to the aqueous phase, a fast homogeneous electron transfer from the tyramine monomer reduces the gold ion. Electropolymerization then proceeds, and gold nanoparticles form. The newly formed nanoparticles act as nucleation sites for the deposition of the oligomers/polymer (and possibly vice versa). This results in gold nanoparticles stabilized in a polytyramine matrix. The size of the nanoparticles is controlled by the concentration of oligomers/polymer in solution. The polymer nanoparticle composite film was analyzed with TEM, XPS, and AFM.     

Gold nanoparticles: catalyst for the oxidation of NADH to NAD(+)

Nicotinamide adenine dinucleotide is an important coenzyme involved in the production of ATP, the fuel of energy, in every cell. It alternates between the oxidized form NAD(+) and the reduced form dihydronicotinamide adenine dinucleotide (NADH) and serves as a hydrogen and electron carrier in the cellular respiratory processes. In the present work, the catalytic effect of gold nanoparticles on the oxidization of NADH to NAD(+) was investigated. The addition of gold nanoparticles was found to quench the NADH fluorescence intensities but had no effect on the fluorescence lifetime. This suggested that the fluorescence quenching was not due to coupling with the excited state, but due to changing the ground state of NADH. The intensity of the 340 nm absorption band of NADH was found to decrease while that of the 260 nm band of NAD(+) was found to increase as the concentration of gold nanoparticles increased. This conversion reaction was further supported by nuclear magnetic resonance and mass spectroscopy. The effect of the addition of NADH was found to slightly red shift and increase the intensity of the surface plasmon absorption band of gold nanoparticles at 520 nm. This gives a strong support that the conversion of NADH to NAD(+) is occurring on the surface of the gold nanoparticles, i.e. NADH is surface catalyzed by the gold nanoparticles. The catalytic property of this important reaction might have important future applications in biological and medical fields.     

A novel extracellular synthesis of monodisperse gold nanoparticles using marine alga, Sargassum wightii Greville

The process of development of reliable and eco-friendly metallic nanoparticles is an important step in the field of nanotechnology. To achieve this use of natural sources like biological systems becomes essential. In the present, work we have investigated extracellular biosynthesis of gold nanoparticles using Sargassum wightii and have achieved rapid formation of gold nanoparticles in a short duration. The UV-vis spectrum of the aqueous medium containing gold ion showed peak at 527 nm corresponding to the plasmon absorbance of gold nanoparticles. Transmission electron microscopy (TEM) showed formation of well-dispersed gold nanoparticles in the range of 8-12 nm. X-ray diffraction (XRD) spectrum of the gold nanoparticles exhibited Bragg reflections corresponding to gold nanoparticles.     

火菇素酪氨酸微区的研究

用紫外差光谱和荧光光谱技术对火菇素的酪氨酸微区进行了研究,结果表明火菇素表现典型的酪氨酸残基紫外275nm吸收峰,ε~m~a~x=20322L·mol^-^1·cm^-^1,紫外差光谱滴定发现,当10.1相似文献   

Tryptophan-based peptides to synthesize gold and silver nanoparticles: a mechanistic and kinetic study

Synthetic oligopeptides with a tryptophan residue at the C-terminus have been used for the synthesis of gold and silver nanoparticles at pH 11. The tryptophan residue in the peptides is responsible for the reduction of metal ions to the respective metals, possibly through electron transfer. A mechanistic pathway has been proposed to explain the reductive properties of the tryptophan moiety of the peptide based on some spectroscopic techniques, such as UV-visible and fluorescence spectroscopy. This study reveals that some of the peptide molecules are converted to its corresponding ditryptophan, kynurenine form and some cross-linked products, all of which are highly fluorescent species. The resultant peptide-functionalized metal nanoparticles have also been characterized by UV-visible spectroscopy, transmission electron microscopy, and Fourier transform IR spectroscopy and thermogravimatric analysis.     

Biosynthesis of anisotropic gold nanoparticles using Maduca longifolia extract and their potential in infrared absorption

Metal nanoparticles, in general, and gold nanoparticles, in particular, are very attractive because of their size- and shape-dependent properties. Biosynthesis of anisotropic gold nanoparticles using aqueous extract of Madhuca longifolia and their potential as IR blockers has been demonstrated. The tyrosine residue was identified as the active functional group for gold ion reduction. These gold nanoparticles were characterized by of UV-Vis spectrophotometer, FTIR, TEM and HrTEM. The presence of proteins was identified by FTIR, SDS-PAGE, UV-Vis and fluorescence spectroscopy. The micrograph revealed the formation of anisotropic gold nanoaprticles. The biologically synthesized gold nanotriangles can be easily coated in the glass windows which are highly efficient in absorbing IR radiations.     

The Radical Ion Chemistry of S-Nitrosylated Peptides

The radical ion chemistry of a suite of S-nitrosopeptides has been investigated. Doubly and triply-protonated ions of peptides NYCGLPGEYWLGNDK, NYCGLPGEYWLGNDR, NYCGLPGERWLGNDR, NACGAPGEKWAGNDK, NYCGLPGEKYLGNDK, NYGLPGCEKWYGNDK and NYGLPGEKWYGCNDK were subjected to electron capture dissociation (ECD), and collision-induced dissociation (CID). The peptide sequences were selected such that the effect of the site of S-nitrosylation, the nature and position of the basic amino acid residues, and the nature of the other amino acid side chains, could be interrogated. The ECD mass spectra were dominated by a peak corresponding to loss of ^?NO from the charge-reduced precursor, which can be explained by a modified Utah-Washington mechanism. Some backbone fragmentation in which the nitrosyl modification was preserved was also observed in the ECD of some peptides. Molecular dynamics simulations of peptide ion structure suggest that the ECD behavior was dependent on the surface accessibility of the protonated residue. CID of the S-nitrosylated peptides resulted in homolysis of the S?CN bond to form a long-lived radical with loss of ^?NO. The radical peptide ions were isolated and subjected to ECD and CID. ECD of the radical peptide ions provided an interesting comparison to ECD of the unmodified peptides. The dominant process was electron capture without further dissociation (ECnoD). CID of the radical peptide ions resulted in cysteine, leucine, and asparagine side chain losses, and radical-induced backbone fragmentation at tryptophan, tyrosine, and asparagine residues, in addition to charge-directed backbone fragmentation.     

The Dominant Role of Oxygen in Modulating the Chemical Evolution Pathways of Tyrosine in Peptides: Dityrosine or Melanin

In diverse biological systems, the oxidation of tyrosine to melanin or dityrosine is crucial for the formation of crosslinked proteins and thus for the realization of their structural, biological, and photoactive functionalities; however, the predominant factor in determining the pathways of this chemical evolution has not been revealed. Herein, we demonstrate for tyrosine‐containing amino acid derivatives, peptides, and proteins that the selective oxidation of tyrosine to produce melanin or dityrosine can be readily realized by manipulating the oxygen concentration in the reaction system. This oxygen‐dependent pathway selection reflects the selective chemical evolution of tyrosine to dityrosine and melanin in anaerobic and aerobic microorganisms, respectively. The resulting melanin‐ and dityrosine‐containing nanomaterials reproduce key functions of their natural counterparts with respect to their photothermal and photoluminescent characteristics, respectively. This work reveals the plausible role of oxygen in the chemical evolution of tyrosine derivatives and provides a versatile strategy for the rational design of tyrosine‐based multifunctional biomaterials.     

In situ synthesis of gold and silver nanoparticles by using redox-active amphiphiles and their phase transfer to organic solvents

An in situ reduction approach to synthesizing gold and silver nanoparticles by using a series of newly designed, redox-active amphiphiles at basic pH is described. These amphiphiles are the conjugates of a fatty acid (e.g., oleic acid, stearic acid, and lauric acid) and a redox-active amino acid (e.g., tryptophan or tyrosine). The amphiphile-coated nanoparticles are then efficiently transferred from water to different nonpolar organic media (such as benzene, toluene, xylene, cyclohexane, and hexane) simply by acid treatment. The phase-transfer process was monitored by UV/visible spectroscopy and transmission electron microscopy, and the results showed that the average particle size and size distribution remain almost unchanged after transferring to the organic media. The anchoring of the amphiphile to the nanoparticle surface was confirmed by FTIR spectroscopy and thermogravimetric analysis. A mechanism is proposed to describe the stability of colloidal Au and Ag nanoparticles formed in situ and their phase transfer to organic solvents. The presence of the amphiphile increases the thermal stability of the colloidal gold nanoparticle conjugates in organic solvents.     

Biosynthesis of Gold Nanoparticles by Streptomyces sp. ERI-3 Supernatant and Process Optimization for Enhanced Production

In this study, we present a simple and eco-friendly method for extracellular biosynthesis of gold nanoparticles by Streptomyces sp. ERI-3 cell-free supernatant. The research was also aimed to evaluate the effects of different reaction parameters including incubation temperature, reaction time, HAuCl₄ concentration and pH on gold nanoparticles production. The UV?CVis spectroscopy was used to monitor the formation of gold nanoparticles. The synthesized gold nanoparticles were characterized with XRD, TEM, and SEM. The average particle size ranged from 10 to 30?nm with spherical shape at optimum conditions.     

AGGREGATION OF COLLAGEN EXPOSED TO UVA IN THE PRESENCE OF RIBOFLAVIN: A PLAUSIBLE ROLE OF TYROSINE MODIFICATION

Riboflavin-sensitized photodynamic modification of collagen led to significant formation of cross-linked molecules. Sodium azide or l,4-diazabicyclo(2,2,2)octane, which are known to be singlet oxygen quenchers, and catalase could not inhibit the modification. Surprisingly, the collagen modification was accelerated in the presence of superoxide dismutase. The aggregation was accompanied by the loss of tyrosine and histidine residues in the collagen. An inhibitory effect of dissolved oxygen on the modification of collagen was observed. Similarly, the loss of tyrosine residues in the irradiated collagen was inhibited in the presence of dissolved oxygen. Dityrosine formation was also observed with the loss of tyrosine. These results indicate that photodynamic modification of tyrosine probably contributes to the riboflavin-sensitized cross-linking of collagen through the formation of dityrosine.     

Biosynthesis of Au nanoparticles using olive leaf extract: 1st Nano Updates

The biological synthesis of gold nanoparticles (AuNPs) of various shapes (triangle, hexagonal, and spherical) using hot water olive leaf extracts as reducing agent is reported. The size and the shape of Au nanoparticles are modulated by varying the ratio of metal salt and extract in the reaction medium. Only 20 min were required for the conversion into gold nanoparticles at room temperature, suggesting a reaction rate higher or comparable to those of nanoparticles synthesis by chemical methods. The variation of the pH of the reaction medium gives AuNPs nanoparticles of different shapes. The nanoparticles obtained are characterized by UV–Vis spectroscopy, photoluminescence, transmission electron microscopy (TEM), X-ray diffraction (XRD), FTIR spectroscopy and thermogravimetric analysis. The TEM images showed that a mixture of shapes (triangular, hexagonal and spherical) structures was formed at lower leaf broth concentration and high pH, while smaller spherical shapes were obtained at higher leaf broth concentration and low pH.     

Electrochemical oxidation and cleavage of peptides analyzed with on-line mass spectrometric detection

An on-line electrochemistry/electrospray mass spectrometry system (EC/MS) is described that allows fast analysis of the oxidation products of peptides. A range of peptides was oxidized in an electrochemical cell by application of a potential ramp from 0 to 1.5 V during passage of the sample. Electrochemical oxidation of peptides was found to occur readily when tyrosine was present. Tyrosine was found to be oxidized between 0.5 and 1.0 V to various oxidation products, including peptide fragments formed by hydrolysis at the C-terminal side of tyrosine. The results confirm earlier knowledge on the mechanisms and reaction products of chemical and electrochemical peptide oxidation. Methionine residues are also readily oxidized, but do not induce peptide cleavage. At potentials higher than about 1.1 V, additional oxidation products were observed in some peptides, including loss of 28 Da from the C-terminus and dimerization. The tyrosine-specific cleavage reaction suggests a possible use of the EC/MS system as an on-line protein digestion and peptide mapping system. In addition, the system can be used to distinguish phosphorylated from unphosphorylated tyrosine residues. Four forms of the ZAP-70 peptide ALGADDSYYTAR with both, either or neither tyrosine phosphorylated were subjected to a 0-1.5 V potential ramp. Oxidation of, and cleavage adjacent to, tyrosine was observed exclusively at unphosphorylated tyrosine residues.