Protein Adsorption on a Glycosylated Polyacrylonitrile Surface: Monitoring with QCM and SPR

Abstract

A simple and efficient method to fabricate a glycosylated surface on a polyacrylonitrile-based film is described. Construction and protein adsorption processes were monitored in situ using a QCM. A PANCHEMA film was deposited on the gold surface of the quartz crystal, and the glycosylated surface was then constructed through surface modification. Con A and BSA were used as probes to study the specificity of this surface to proteins. It can recognize Con A, while showing no specific interaction with BSA. The binding affinity indicates the presence of strong multivalent interactions between Con A and the glucose residues (cluster glycoside effect). Reproducibility and repeatability of the glycosylated polymer surface are sufficient to allow specific adsorption of Con A.

Hybrid Material for Protein Sensing Based on Electrosynthesized MIP on a Mannose Terminated Self‐Assembled Monolayer

“…The dissociation constant ( K d ) of 1.42 μ m is determined using the Langmuir adsorption model. The value is in the same range with the previous reports on various types of mannose SAM and lower than that obtained from monovalent sugar/protein interaction by two to three orders of magnitude representing the multivalent binding of ConA to the mannose surface. The adsorption of ConA has reached its saturation at around 0.84 μg cm −2 which corresponds to a perfect monolayer coverage as calculated using the Sauerbrey equation and the geometrical surface area of ConA estimated from its crystallographic structure (24.37 nm 2 ).…”

Studying the interaction of carbohydrate–protein on the dendrimer-modified solid support by microarray-based plasmon resonance light scattering assay

“…evaluated by the approach since the interaction of Con A with mannose/glucose has been studied extensively using many methods and techniques. 10,15,16 Here, different concentrations of Man-a were spotted on the slide and probed with various concentrations of biotin-Con A, respectively. Because the RLS intensity for each array component at a given Man-a concentration can vary as a function of the concentration of Con A, the assay can be used for evaluating the K D,surf of lectin with immobilized carbohydrate (as shown in Fig.…”

“…[1][2][3][4][5][6][7][8][9] Therefore, a better understanding of glycoconjugate-protein interactions would greatly aid in the elucidation of intercellular signaling pathways and the development of new diagnostic and therapeutic methods. 8,9 Under these circumstances, glycoconjugate-protein interactions have been investigated by various techniques, such as surface plasmon resonance (SPR), 10,11 affinity chromatography/capillary electrophoresis, 12,13 quartz crystal microbalance (QCM), 14,15 isothermal titration calorimetry (ITC) 16,17 and carbohydrate microarray. [18][19][20] In particular, carbohydrate microarrays provide a high-throughput tool to evaluate many potential carbohydrate-protein interactions in parallel while using only minuscule amounts of scarce materials.…”

Virus-Poly(3,4-ethylenedioxythiophene) Biocomposite Films

“…Quartz crystal microbalance (QCM) gravimetry 29–33 and coulometry permit this correlation to be established. Second, determine the influence of virus particles in the polymerization solution on the rate of the electropolymerization process.…”