Analytical and Bioanalytical Chemistry

, Volume 400, Issue 8, pp 2499–2506 | Cite as

Surface molecular imprints of WGA lectin as artificial receptors for mass-sensitive binding studies

  • Thipvaree Wangchareansak
  • Chak Sangma
  • Kiattawee Choowongkomon
  • Franz Dickert
  • Peter LieberzeitEmail author
Original Paper


Wheat germ agglutinin (WGA) lectin is a model compound for the interaction between viruses and cells during infection events and thus an interesting analyte for mass-sensitive sensing to study these interaction phenomena. Scanning tunneling microscopy studies reveal that surface molecular imprinting leads to cavities having the dimensions of WGA dimers. These reincorporate WGA from phosphate-buffered saline between 1 and 160 μg/ml. Whereas the quartz crystal microbalance (QCM) frequency for molecularly imprinted polymer (MIP)-coated electrodes decreases, indicating uptake of the analyte, their nonimprinted counterparts yield positive, concentration-dependent frequency shifts characteristic for slip of the analyte on the QCM surface. The MIPs achieve selectivity factors towards bovine serum albumin of roughly 4 at higher protein concentrations. Brunauer-Emmett-Teller analysis reveals that binding is favored by 29 kJ/mol until the adsorption of up to ten monolayers on the MIP, whereas above this range the value is lower. Together with the binding behavior of MIP and nonimprinted polymers, this indicates that the MIP acts as a nucleus for multilayer deposition onto the surface.


Wheat germ agglutinin lectin Molecular imprinting Quartz crystal microbalance Brunauer–Emmett–Teller analysis 



Financial support by the Royal Golden Jubilee Grant Foundation, the Thai Research Fund (TRF), Bilateral Research Cooperation (BRC), Faculty of Science, Kasetsart University, and ASEA UNINET is gratefully acknowledged.


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Copyright information

© Springer-Verlag 2011

Authors and Affiliations

  • Thipvaree Wangchareansak
    • 1
    • 2
  • Chak Sangma
    • 2
  • Kiattawee Choowongkomon
    • 3
  • Franz Dickert
    • 1
  • Peter Lieberzeit
    • 1
    Email author
  1. 1.University of Vienna, Department of Analytical ChemistryViennaAustria
  2. 2.Department of Chemistry, Faculty of ScienceKasetsart UniversityBangkokThailand
  3. 3.Department of Biochemistry, Faculty of ScienceKasetsart UniversityBangkokThailand

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