The affinity of monoclonal antibodies can be measured accurately because they are homogeneous and selective for a single epitope. K A can therefore vary widely for antibodies from below 10 5 mol -1 to above 10 12 mol -1, and can be influenced by factors including pH, temperature and buffer composition. However, high-affinity antibodies will bind a greater amount of antigen in a shorter period of time than low-affinity antibodies.
The time taken for this to occur depends on rate of diffusion and is similar for every antibody. In other words, K A describes how much antibody-antigen complex exists at the point when equilibrium is reached. = molar concentration of the antibody-antigen complex.= molar concentration of unoccupied binding sites on the antigen.= molar concentration of unoccupied binding sites on the antibody.It is defined by the same basic thermodynamic principles that govern any reversible biomolecular interaction: When describing the strength of the antigen-antibody complex, affinity and avidity are always mentioned.Īffinity measures the strength of interaction between an epitope and an antibody’s antigen binding site.
Antigen-antibody interactions are non-covalent and reversible, formed by a combination of hydrogen bonds, hydrophobic interactions, electrostatic and van der Waals forces.
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