The emergence of molecular imprinting has its original source in the area of immunology. By the early 1930s Breinl and Haurowitz, followed by Mudd, proposed a theory for the diversity of antibody formation in their encounter with xenobiotic antigens. The remarkable specificity of antibody-antigen complexes, found in, e.g. the chiral recognition of d- and l-tartranilic acid was attributed to the interactions of the chemical groupings of the nascent antibody with the antigen during antibody biosynthesis. Each structural unit of the antibody would be selected and oriented, at the moment of synthesis, to fit the local configuration and features of the antigen surface. These theoretical considerations were further elaborated by Pauling, who postulated that the great diversity in antibody formation was due to the formation of different three-dimensional configurations of the antibody polypeptide chain induced by the interaction with the antigens. Following these “instructive” theories on antibody diversity, the antibodies would be able to change their 3-D-structure in order to form as many interaction points as possible with the epitopes of the antigens. Thus, the antibody combining sites were “moulded” with the antigen as a template in a casting procedure, i.e. they were molecularly imprinted with the antigens (Figure 2).
Later, these theories were found to be incorrect and their instructive models abandoned in favour of the more appropriate “clonal selective” theory of antibody formation. Nevertheless, their models laid the foundations for the area of molecular imprinting.
Adopted from www.smi.tu-berlin.de
