Tag Archives: antibody affinity
Effect of trifluoroethanol on antibodies binding properties
S. A. Bobrovnik*, M. O. Demchenko, S. V. Komisarenko
Department of Molecular Immunology, Palladin Institute of Biochemistry,
National Academy of Sciences of Ukraine, Kyiv;
*e-mail: s-bobrov@ukr.net
Received: 01 December 2022; Revised: 22 February 2023;
Accepted: 13 April 2023; Available on-line: 27 April 2023
The studies on the influence of organic co-solvents on the structure and function of antibodies are of key interest, especially in view of antibodies broad use as recognizing elements in different analytical systems. Here we studied the effect of co-solvent 2,2,2-trifluoroethanol (TFE) on the ability of anti-ovalbumin monoclonal antibodies to interact with its specific antigen. Antibody affinity to antigen and the rate constants of antibody binding to immobilized antigen were analyzed. Changes in antibody reactivity with incubation time which depended on TFE concentration and temperature were revealed. When treatment of antibodies with TFE was carried out at 0°C, we observed nonlinear, non-monotonous changes of antibody reactivity with initial fast decrease and substantial increase as incubation continued that may be related to the loss of antigen binding reactivity by some part of antibodies at the start but its restoration when the incubation proceeds.
Effect of trifluoroethanol on antibody reactivity against corresponding and nonrelated antigens
S. A. Bobrovnik, M. O. Demchenko, S. V. Komisarenko
Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;
e-mail: s-bobrov@ukr.net
The ability of antibodies to switch between specific and nonspecific recognition of antigens under various factors is the key issue. Here we demonstrate that 2,2,2-trifluoroethanol (TFE) is one of these factors influencing the ability of monoclonal antibodies to react specifically with corresponding antigen (ovalbumin) and transforming them into polyreactive immunoglobulins (PRIGs) that are strong but nonspecific binders with various antigens. Such switching of antibody reactivity is nonlinear and even nonmonotonous function of TFE concentration and depends strongly on incubation time and temperature. At room temperatures (25 °C) the specific antibodies under 30% TFE action are transformed into PRIGs. However, at 0 °C the variation of antibody reactivity is complicated. TFE is known as the alcohol with one of the strongest proton-donor abilities in hydrogen bonding and its effect is probably in binding to specific sites that switch the antibody recognition ability.