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Sökning: WFRF:(Makaraviciute Asta) > (2014)

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1.
  • Makaraviciute, Asta, et al. (författare)
  • A QCM-D Study of Reduced Antibody Fragments Immobilized on Planar Gold and Gold Nanoparticle Modified Sensor Surfaces
  • 2014
  • Ingår i: Key Engineering Materials. - : Trans Tech Publications. - 1013-9826 .- 1662-9795. ; 605, s. 340-343
  • Tidskriftsartikel (refereegranskat)abstract
    • An immunosensor is an analytical system consisting of specific immune system molecules coupled to a signal transducer. Immunosensor sensitivity depends on the type of immunorecognition ligands used, immobilization influence on their activity and orientation on the surface. Quartz crystal microbalance with dissipation (QCM-D) was employed to investigate the immobilization of antibodies against bovine leukemia virus antigen gp51 (gp51). Disulphide bridges of antibody hinge region were reduced chemically to yield two “half” antibody fragments (Frag-Ab), each having a single antigen binding site and free sulfhydryl groups that were used for immobilization. Frag-Ab were immobilized on planar gold and gold nanoparticle (AuNP) modified QCM-D sensor surfaces from initial solutions of different concentrations. Higher Frag-Ab surface density values were obtained on AuNP modified surfaces at all tested antibody concentrations. Frag-Ab/gp51 specific interaction was registered and it was determined that the highest sensitivity was exhibited by Frag-Ab immobilized at the lowest surface desities on both types of investigated surfaces. Specific gp51 interaction with Frag-Ab and non-specific binding to bovine serum albumin modified surfaces were
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2.
  • Makaraviciute, Asta, et al. (författare)
  • Antibody fragment immobilization on planar gold and gold nanoparticle modified quartz crystal microbalance with dissipation sensor surfaces for immunosensor applications
  • 2014
  • Ingår i: Analytical Methods. - : Royal Society of Chemistry. - 1759-9660 .- 1759-9679. ; 6:7, s. 2134-2140
  • Tidskriftsartikel (refereegranskat)abstract
    • Immunosensors are bioaffinity sensors incorporating immune system molecules that are utilized for analyte recognition and signal transduction yielding a measurable signal upon analyte detection. A lot of effort has been made to optimize the immobilization matrix on the sensor surface since the outcome of the ligand immobilization procedure determines sensitivity, specificity and longevity of the developed immunosensor. In this work, antibodies against bovine leukemia virus antigen gp51 were chemically reduced to "half" antibody fragments that were later employed as recognition ligands. Antibody fragments at different concentrations were immobilized via thiolate bonds on planar gold and gold nanoparticle modified surfaces of a quartz crystal microbalance with dissipation sensor. Antibody fragment immobilization and interaction with antigen were investigated. Antibody fragment surface mass densities after the immobilization on planar gold and gold nanoparticle modified sensor surfaces were directly dependent on the initial antibody concentration. The highest analytical response was exhibited by antibody fragments immobilized at the smallest surface mass density on planar gold and gold nanoparticle modified surfaces. Bovine leukemia virus antigen gp51 interaction with antibody fragments was compared with non-specific gp51 interaction with bovine serum albumin on planar gold and gold nanoparticle modified surfaces by employing Delta D/Delta f plots.
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  • Resultat 1-2 av 2
Typ av publikation
tidskriftsartikel (2)
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refereegranskat (2)
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Ruzgas, Tautgirdas (2)
Makaraviciute, Asta (2)
Ramanavicius, Arunas (2)
Ramanaviciene, Almir ... (2)
Lärosäte
Malmö universitet (2)
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Engelska (2)
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