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Träfflista för sökning "WFRF:(Xie Bin) srt2:(2000-2004)"

Sökning: WFRF:(Xie Bin) > (2000-2004)

  • Resultat 1-9 av 9
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1.
  • Liang, Z P, et al. (författare)
  • Electrochemical study of the XNA on Gold (TM) microarray
  • 2004
  • Ingår i: Biosensors & Bioelectronics. - : Elsevier BV. - 1873-4235 .- 0956-5663. ; 20:2, s. 211-216
  • Tidskriftsartikel (refereegranskat)abstract
    • A novel electrode array was developed based on the XNA on Gold(TM) microarray platform. The platform combines self-assembling monolayers, thick film patterning and streptavidin based immobilization to provide a robust, versatile platform capable of analysing virtually any biomolecule including nucleic acids, proteins, carbohydrates and lipids. Electrochemical analysis of the self-assembling monolayer/streptavidin (SAMS) XNA on Gold(TM) coating revealed that the ferrocene redox current for the SAMS modified electrode was greater than that with a bare Gold(TM) electrode. The electrochemical reaction of K4Fe(CN)(6) was inhibited by the SAMS coating, but was reactivated upon addition of ferrocene. These results indicate that ferrocene is involved as a mediator in the electron transfer of K4Fe(CN)(6) to the SAMS modified electrode. Addition of DNA to the SAMS resulted in only a minor change in the electrochemical signal, indicating that XNA on Gold(TM) can be used for electrochemical based bioanalysis. After cycling a SAMS electrode 50 times, no signs of deterioration were detected showing that coating has excellent stability. In addition to the biosensing applications, the scheme provides a non-invasive method for accessing the quality of the SAMS coatings which is of industrial interest. These studies show that the XNA on Gold(TM) microarray platform can be used for electrochemical studies, thus providing an additional alternative for developing multianalyte biosensors as well as expanding the range of detection methods available for microarray analysis. (C) 2004 Elsevier B.V. All rights reserved.
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2.
  • Xie, Bin (creator_code:cre_t)
  • [An optical circulation amplification type biological chip detecting process]
  • 2004
  • Patent (övrigt vetenskapligt/konstnärligt)abstract
    • The invention discloses an optical circulation enlarged type biological chip detecting method, wherein the enzyme recirculation and bioluminescence are combined, for realizing the FMNH#-[2] accumulation through the circulation on the electrodes by the NADH/NAD#+[+] oxidation-reduction, the high level accumulation FMNH#-[2] reacts with other light-emitting bottom luciferase, long chain aldehydes and oxygen, giving off fluorescent light having wavelength of 490nm. The invention realizes high sensibility, low cost and simplicity of operation, thus is suitable for each types of biological sample analysis.
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3.
  • Xie, Bin (creator_code:cre_t)
  • 氨酰基转运核糖核酸合成酶识别型蛋白芯片的制备方法
  • 2004
  • Patent (övrigt vetenskapligt/konstnärligt)abstract
    • A method of manufacturing a protein chip for identifying aminoacyl-tRNA synthetases, suitable for detecting basic amino acids in proteins. It is characterized in, immoblizing aminoacyl-tRNA synthetases corresponding to 20 basic amino acids in arrays onto the surface of the chip, then fixing 20 kinds of tRNAs labelled by fluorescence onto the corresponding synthetases, then obtaining a chip of aminoacyl-tRNA synthetases. The chip could detect amino acids in proteins. By scanning fluorescence, amino acids in proteins will be determined based on fluorescence of 20 wells.
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4.
  • Danielsson, Bengt, et al. (författare)
  • Trends in Calorimetric Biosensors
  • 2002
  • Ingår i: Proceedings of the Sensor Symposium on Sensors, Micromachines, and Applied Systems. ; 19, s. 7-12
  • Konferensbidrag (refereegranskat)
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5.
  • Mecklenburg, Michael, et al. (författare)
  • A Microarray platform for "omics" analysis
  • 2001
  • Ingår i: International Conference on Sensor Technology (ISTC 2001). - : SPIE. - 0277-786X. - 0819441198 - 9780819441195 ; 4414, s. 157-163
  • Konferensbidrag (refereegranskat)abstract
    • Microarray technology has revolutionized genetic analysis. However, limitations in genome analysis has lead to renewed interest in establishing 'omic' strategies. As we enter the post-genomic era, new microarray technologies are needed to address these new classes of 'omic' targets, such as proteins, as well as lipids and carbohydrates. We have developed a microarray platform that combines self- assembling monolayers with the biotin-streptavidin system to provide a robust, versatile immobilization scheme. A hydrophobic film is patterned on the surface creating an array of tension wells that eliminates evaporation effects thereby reducing the shear stress to which biomolecules are exposed to during immobilization. The streptavidin linker layer makes it possible to adapt and/or develop microarray based assays using virtually any class of biomolecules including: carbohydrates, peptides, antibodies, receptors, as well as them ore traditional DNA based arrays. Our microarray technology is designed to furnish seamless compatibility across the various 'omic' platforms by providing a common blueprint for fabricating and analyzing arrays. The prototype microarray uses a microscope slide footprint patterned with 2 by 96 flat wells. Data on the microarray platform will be presented.
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6.
  • Mecklenburg, M., et al. (författare)
  • Differentiation of human serum samples by surface plasmon resonance monitoring of the integral glycoprotein interaction with a lectin panel
  • 2002
  • Ingår i: Analytica Chimica Acta. - 0003-2670 .- 1873-4324. ; 459:1, s. 25-31
  • Tidskriftsartikel (refereegranskat)abstract
    • Bacterial infection and inflammation result in massive changes in serum glycoproteins. These changes were investigated by the interaction of the saccharide glycoprotein moiety with lectins. A panel of eight lectins (Canavalia ensiformis, Bandeiraea simplicifolia BS-I, Arachis hypogaea, Phytolacca americana, Phaseolus vulgaris, Artocarpus integrifolia, Triticum vulgaris and Pisum sativum) was used to differentiate human serum glycoproteins obtained from patients with various bacterial infections. Lectin functionalised sensing layers were created on gold-coated wafers and lectin-glycoprotein interactions were monitored by surface plasmon resonance. The interaction of the lectin panel with serum glycoproteins produces unique patterns. Principal component analysis (PCA) was used to analyse the patterns. The actual panel of eight lectins enabled discrimination between sera obtained from patients sick with bacterial infection and healthy patients. Extended lectin panels have the potential to distinguish between types of bacterial infection and identify specific disease state. © 2002 Elsevier Science B.V. All rights reserved.
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7.
  • Meng, Qinglai, et al. (författare)
  • Development of a tRNA-Synthetase Microarray for Protein Analysis
  • 2004
  • Ingår i: Sensors and Materials. - 0914-4935. ; 16:8, s. 401-412
  • Tidskriftsartikel (refereegranskat)abstract
    • Proteins are composed of 20 different amino acids. In the translation process, each of these 20 amino acids is specifically recognized by their cognate aminoacyl-tRNA synthetase. The fidelity of this recognition system is essential if translation is to function properly. The development of an in vitro system based on this recognition scheme would make a powerful analytical tool with which to analyse translation, as well as providing an additional biomimetic scheme for protein analysis. Aminoacyl-tRNA synthetases microarrays could be applied to protein fingerprinting and sequence analysis. The fabrication of aminoacyl-tRNA synthetase arrays requires the use of advanced protein arraying technology that has only recently become available. In order to demonstrate the feasibility of this scheme, glutamyl-tRNA synthetase (GluRS) was immobilized on the streptavidinbased XNA on GoldTM biochip platform. The streptavidin layer provides a simple, efficient immobilization scheme that reduces nonspecific binding and improves the biocompatibility of the surface. Here, we demonstrate that biotinylated GluRS can be successfully immobilized on XNA on GoldTM. The immobilization efficiency was determined by double labelling GluRS with biotin and the fluorescent label Cy5. The CCD fluorescent microscopy images revealed that the GluRS was efficiently immobilized and evenly distributed over the surface. Control experiments indicate a very low degree of nonspecific binding which is essential if detection of these multicomponent, low-affinity interactions is to be realized. Furthermore, we show that immobilization does not significantly reduce the function of the enzyme. In addition to the specific aims of this study, this technology would provide valuable insights into the biomechanics of translation as well as being a tool for studying tRNA modifications and subclasses. Moreover, the implications for developing coupled transcription and translation systems should not be overlooked. Protein analysis schemes based on this approach would provide an urgently needed compliment to traditional methods. Finally, these arrays might also be useful tools in our efforts to understand the regulatory functions that small RNAs, i.e., iRNA, have been shown to play.
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8.
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9.
  • Xie, Bin, et al. (författare)
  • Mini/micro thermal biosensors and other related devices for biochemical/clinical analysis and monitoring
  • 2000
  • Ingår i: TrAC - Trends in Analytical Chemistry. - 0165-9936. ; 19:5, s. 340-349
  • Tidskriftsartikel (refereegranskat)abstract
    • The present review discusses the recent developments in the design, fabrication and implementation of mini/micro thermal biosensors for biochemical/clinical analysis and monitoring. The principle of thermometric sensing and recent developments in microfabrication technology are introduced, followed by their adaptation to thermometric devices. The instrumentation of the mini, micro and multisensing thermometric devices are described followed by their application to a variety of biochemical/clinical analyses. Other developments in material design and hybrid devices for thermometric sensing are also mentioned.
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