Specific binding of large aggregates of amphiphilic molecules to the respective antibodies

NABOK, A. V., TSARGORODSKAYA, A., HOLLOWAY, A., STARODUB, N. F. and DEMCHENKO, A. (2007). Specific binding of large aggregates of amphiphilic molecules to the respective antibodies. Langmuir, 23 (16), 8485-8490.

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Link to published version:: https://doi.org/10.1021/la700414z


The Binding of nonylphenol to respective antibodies immobilized on solid substrates was studied with the methods of total internal reflection ellipsometry (TIRE) and QCM (quartz crystal microbalance) impedance spectroscopy. The binding reaction was proved to be highly specific having an association constant of K-A = 1.6 x 10(6) mol(-1) L and resulted in an increase in both the adsorbed layer thickness of 23 nm and the added mass of 18.3 mu g/cm(2) at saturation. The obtained responses of both TIRE and QCM methods are substantially higher than anticipated for the immune binding of single molecules of nonylphenol. The mechanism of binding of large aggregates of nonylphenol was suggested instead. Modeling of the micelle of amphiphilic nonylphenol molecules in aqueous solutions yielded a micelle size of about 38 nm. The mechanism of binding of large molecular aggregates to respective antibodies can be extended to other hydrophobic low-molecular-weight toxins such as T-2 mycotoxin. The formation of large molecular aggregates of nonylphenol and T-2 mycotoxin molecules on the surface was proved by the AFM study.

Item Type: Article
Research Institute, Centre or Group - Does NOT include content added after October 2018: Materials and Engineering Research Institute > Advanced Coatings and Composites Research Centre > Electronic Materials and Sensors Research Group
Identification Number: https://doi.org/10.1021/la700414z
Page Range: 8485-8490
Depositing User: Ann Betterton
Date Deposited: 31 Mar 2010 15:43
Last Modified: 18 Mar 2021 21:30
URI: https://shura.shu.ac.uk/id/eprint/1443

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