904 resultados para PLASMON RESONANCE SPECTROSCOPY


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Nanocomposite films consisting of nanosized Ag particles embedded in partially oxidized amorphous Si-containing matrices were prepared by radio frequency magnetron co-sputtering deposition. We studied the influence of ambient atmosphere during the preparation and heat-treatment of Ag/SiOx (0 less than or equal to x less than or equal to 2) nanocompositefilm on its optical absorption properties. We found that the plasmon resonance absorption peak shifts to shorter wavelengths with the increasing oxygen content in the SiOx matrix. The analysis indicates that the potential barrier between Ag nanoparticles and SiOx matrix increases with the increasing x value, which will induce the surface resonance state to shift to higher energy. The electrons in the vicinity of the Fermi level of Ag nanoparticles must absorb more energy to be transferred to the surface resonance state with the increasing x value. It was also found that the plasmon resonance absorption peaks of the samples annealed in different ambient atmospheres are located at about the same position. This is because the oxidation surface layer is dense enough to prevent the oxygen from penetrating into the sample to oxidize the silicon in the inner layer.

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Surface and bulk plasmon resonance of noble metal particles play an essential role in the multicolor photochromism of semiconductor systems containing noble metal particles, Here we examined several key parameters affecting surface plasmon resonance wavelength (SPRW) of Ag particles and investigated the relation between surface plasmon and photochromic reaction wavelength. From the transmission spectra of sandwiched (TiO2/Ag/TiO2) and overcoated (Ag/TiO2) films deposited on quartz substrates at room temperature by rf helicon magnetron sputtering, we demonstrated that the SPRW can be made tunable by changing the surrounding media and thickness of the metal layer. The coloration and bleaching in visible light region due to photochromism were clearly observed for the films inserted with a 0.55 nm Ag layer.

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The plasmon resonance absorption of the Ag/SiO2 nanocomposite film is investigated. The measured absorption spectra are compared with those calculated by the Mie theory. The results indicate that the Mie theory on the basis of classical electrodynamics can only partially explain the optical absorption spectra of the Ag/SiO2 nanocomposite film. We believe that the plasmon resonance absorption is mainly an intrinsic quality of the metal particle, and can be explained only with the electronic structure of the metal particle. In the latter, surface resonance state is introduced to systematically discuss the optical absorption spectra of the Ag/SiO2 nanocomposite film. (C) 2003 Elsevier Science B.V. All rights reserved.

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Based on the multidomain structure of Pseudomonas aeruginosa exotoxin A, a fusion protein termed rPEA has been constructed, which is expected to serve as a gene carrier in vitro. The expression and purification of rPEA are described. The basal properties of rPEA as a gene carrier are evaluated by investigating its interaction with plasmid DNA and mimic biomembrane by surface plasmon resonance (SPR) and electrochemical methods. rPEA is proved to be able to bind with plasmid DNA with high affinity. It can also interact with lipid membrane and increase permeability of the membrane, so the probe molecules can easily reach the gold surface and exhibit the electrochemical response.

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Alternate layer-by-layer (L-by-L) polyion adsorption onto gold electrodes coated with chemisorbed cysteamine gave stable, electroactive multilayer films containing calf thymus double stranded DNA (CT ds-DNA) and myoglobin (Mb). Direct, quasi-reversible electron exchange between gold electrodes and proteins involved the Mb heme Fe2+/Fe3+ redox couple. The formation of L-by-L (DNA/Mb), films was characterized by both in situ surface plasmon resonance (SPR) monitoring and cyclic voltammetry (CV). The effective thickness of DNA and Mb monolayers in the (DNA/Mb)l bilayer were 1.0 +/- 0.1 and 2.5 +/- 0.1 mn, corresponding to the surface coverage of similar to65% and similar to89% of its full packed monolayer, respectively. A linear increase of film thickness with increasing number of layers was confirmed by SPR characterizations. At pH 5.5, the electroactive Mb in films are those closest to the electrode surface; additional protein layers did not communicate with the electrode. CV studies showed that electrical communication might occur through hopping conduction via the electrode/base pair/Mb channel, thanks to the DNA-Mb interaction. After the uptake of Zn2+, a special electrochemical behavior, where MbFe(2+) acts as a DNA-binding reduction catalyst in the Zn2+-DNA/Mb assembly, takes place.

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A surface plasmon resonance (SPR) biosensor was used for the first time to determine the concentration of ferritin in both HBS-EP buffer and serum. The monoclonal antibody was immobilized on the carboxymethyl dextran-modified gold surface by an amine coupling method. The interaction of antibody with antigen was monitored in real-time. The signal was enhanced by sandwich amplification strategy to improve the sensitivity and specificity of the immunoassay, especially in serum. The linear range of the assay in serum is over 30-200 ng ml with the detection limit of 28 ng ml(-1). The sensitivity, specificity, and reproducibility of the assay are satisfactory. The analyte and enhancement antibody-binding surface could be regenerated by pH 2.0 glycine-HCl buffer and the same antibody-immobilized surface could be used for more than 50 cycles of ferritin binding and regeneration.

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The dynamic interaction process of calmodulin with an immobilized peptide melittin was investigated in real time by surface plasmon resonance spectroscopy, and dissociation constant of the complex was calculated to be 3.37 x 10(-6) mol/L.

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Using an enhanced surface plasmon resonance (SPR) immunosensor, we have determined the concentration of human complement factor 4 (C4). Antibody protein was concentrated into a carboxymethyldextran-modified gold surface by electrostatic attraction force and a simultaneous covalent immobilization of antibody based on amine coupling reaction took place. The sandwich method was applied to enhance the response signal and the specificity of antigen binding assay. The antibody immobilized surface had good response to C4 in the range of 0.02-20 mug/ml by this enhanced immunoassay. The regeneration effect by pH 2 glycine-HC1 buffer was also investigated. The same antibody immobilized surface could be used more than 80 cycles of C4 binding and regeneration. In addition, the ability to determinate C4 directly from serum sample without any purification was investigated. The sensitivity, specificity and reproducibility of the enhanced immunoassay are satisfactory. The results clearly demonstrate the advantages of the enhanced SPR technique for C4 immunoassay.

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The high-field nuclear magnetic resonance (NMR) spectra can be used for the rapid multicomponent analysis in small amounts of biological fluids. In this paper, the effect of La (NO3)(3) on the rats' metabolism in urine was investigated by H-1 NMR analysis. The experimental groups of wistar rats were injected intraperitoneally with La(NO3)(3) at doses of 0.2, 2.0, 10 and 20mg/kg body weight. The remarkable variation of low molecular weight metabolites in urine has been identified by H-1 NMR spectra, in which dimethylamine, N, N-dimethylglycine, urea, alpha -ketoglutarate, trimethylamine N-oxide, succinate, citrate and amino acids have been suggested as NMR markers for renal damage and ethanol, lactate, taurine as the markers for liver damage. This work may assess its possible use in the early detection of biochemical changes associated with Rare Earth induced kidney and liver dysfunction.

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A surface plasmon resonance biosensor has been used to determine antibody activity in serum. As a model system, the interaction of mouse IgG and sheep anti-mouse IgG polyclonal antibody was investigated in real time. The factors, including pH value, ionic strength, protein concentration, influencing electrostatic adsorption of mouse IgG protein onto carboxylated dextran-coated sensor chip surface, were studied. The procedures of mouse IgG protein immobilization and immune reaction were monitored in real time. The regeneration effect using the different elution reagents was also investigated. The same mouse IgG immobilized surface can be used for 100 cycles of binding and elution with only 0.38% loss per regeneration in reactivity. The results show that the surface plasmon resonance biosensor is a rapid, simple, sensitive, accurate and reliable detection technique for real-time immunoassay of antibody activity. The assay allows antibodies to be detected and studied in their native form without any purification. (C) 2000 Elsevier Science B.V. All rights reserved.

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The biosensor based on surface plasmon resonance(SPR) technology is a very useful tool to study the interaction between biomolecles. The main advantages of this technique is to "visualize" macromolecular interactions directly in real time, and in a label-free mode rather than indirect methods like enzyme-linked immunosorbent assays (ELISAs). We immobilize human serum albumin (HSA) to the carboxymethyldextran-modified sensor chip surface covalently to detect the activity of anti-HSA in serum, and regenerate the surface with .1 mol/L phosphoric acid. The results show that SPR biosensor can detect the activity of anti-HSA in real-time quickly and the sensor chip can be used over 100 cycles.

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In this paper, the water relaxation enhancement behavior of Gd-diethylenetriamine pentaacetic acid(DTPA) in water and in aqueous solution of bovine serum albumine(BSA) has been studied. The T-1 relaxivity of Gd-DTPA in BSA solution is higher than that in aqueous solution. The results indicate that Gd-DTPA can integrate non-covalently with BSA mainly in forms of (Gd-DTPA) . BSA, (Gd-DTPA)(2) . BSA, for which the apparent equilibrium constant is 0.026 mmol(-1).L,0.0018 mmol(-2).L-2 respectively. This method would be used to study the interactivities between protein and contrast agent.

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The elucidation of key influence factors for electrostatic adsorption is very important to control protein nonspecific adsorption on modified surfaces. In this study, real-time surface plasmon resonance technique is used to characterize the electrostatic adsorption of two proteins (mouse IgG and protein A) on carboxymethyldextran-modified surface. The results show that protein solution pH and ionic strength are key influence factors for efficient electrostatic adsorption. The influence of protein, solution pH on the amount of electrostatic adsorption depends on the type of the charge and the charge density of both protein and modified matrix on the surface. The electrostatic adsorption process involves a competition between the positively charged protein and other positively charged species in the buffer solution. A decrease of ionic strength leads to an increasing electrostatic adsorption. The kinetic adsorption constants of protein A at different pH values were also calculated and compared.

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The assembly of alternating DNA and positively charged poly(dimethyldiallylammonium chloride) (PDDA) multilayer films by electrostatic layer-by-layer adsorption has been studied. Real time surface plasmon resonance (BIAcore) technique was used to characterize and monitor the formation of multilayer films in solution in real time continuously. The results indicate that the uniform multilayer can be obtained on the poly(ethylenimine) (PEI) coated substrate surface. The kinetics of the adsorption of DNA on PDDA surface was also studied by real-time BIAcore technique, and the observed rate constant was calculated using a Langmuir model (k(obs) = (1.28 +/- 0.08) x 10(-2) s(-1)).