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The specific interactions between bovine serum albumin and poly- or two monoclonal bovine serum albumin antibodies were studied using force spectroscopy mode of atomic force microscopy. The histograms of the unbinding forces for polyclonal bovine serum albumin antibodies are broad at high antibody concentrations (50 or 270 μg/ml) and narrow at low concentrations (10 or 27 μg/ml), while the histograms for monoclonal antibodies peak at well defined unbinding force. The peak unbinding force depends on the type of antibody and the antibody concentration. In this paper we described and characterized the passive adsorption and covalent immobilization of proteins for tip and sample preparation. Force spectroscopy could serve as a useful method for characterization of antigen-antibody interactions for measuring the specificity of an antibody or to assess the purity of a monoclonal antibody solution and to distinguish between different antibodies.
EN
In this work the interaction of lysozyme fibrils with magnetic particles has been studied by atomic force microscopy. The experiments were carried out for a better understanding of the binding process of such complex soft matter systems. The obtained results show that interaction between lysozyme fibrils and magnetic particles starts immediately after mixing them together. Moreover, the samples remain stable in duration of several days after preparation.
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