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Title: Self-assembled glucosamine monolayers as biomimetic receptors for detecting WGA lectin and influenza virus with a quartz crystal microbalance
Authors: Thipvaree Wangchareansak
Chak Sangma
Paiboon Ngernmeesri
Arunee Thitithanyanont
Peter A. Lieberzeit
Universitat Wien
Kasetsart University
Mahidol University
Keywords: Biochemistry, Genetics and Molecular Biology;Chemistry
Issue Date: 1-Aug-2013
Citation: Analytical and Bioanalytical Chemistry. Vol.405, No.20 (2013), 6471-6478
Abstract: N-Acetylglucosamine (GlcNAc) is a natural ligand that interacts with the binding sites of wheat germ agglutinin (WGA) lectin. For immobilization, GlcNAc was linked to p-nitrophenol, and the nitro group was reduced and then bound to cysteine via two-step synthesis. Scanning tunneling microscopy studies revealed proper immobilization of the ligand on the gold surface of a quartz crystal microbalance (QCM) via the cysteine S-H bond as well as binding between GlcNAc and WGA. QCM measurements revealed that maximum sensitivity towards WGA can only be achieved when co-immobilizing one part ligand and 5,000 parts cysteine for steric reasons, because it allows binding of a protein monolayer on the surface. Langmuir-type treatment of the binding isotherm suggests two different binding ranges for WGA and the GlcNAc monolayer, because at concentrations of WGA below 1 μm the Gibbs energy for the binding process is one third higher than that at concentrations above this value. The same systems can be transferred to first proof-of-concept measurements with different strains of influenza A virus (H5N3, H5N1, H1N3) because GlcNAc is part of the oligosaccharide ligand responsible for the first binding step. Thus, it constitutes both a suitable tool for rapid analysis and the basis for future theoretical calculations of ligand-virus interactions. © 2013 Springer-Verlag Berlin Heidelberg.
ISSN: 16182650
Appears in Collections:Scopus 2011-2015

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