Sample Research Paper
“ First constant domains (CH1 and CL) of an antibody, Fab chains, as well as leucine zipper motifs derived from the Fos and Jun transcription factors, were used successfully to generate so-called ‘mini-antibodies’. These intermediate-sized Bispecific antibodies, larger than Fab and smaller than whole antibodies, may combine the high tissue penetration of small molecules with the slower whole-body clearance of larger molecules, and hence may represent a better format for therapeutic applications” (Zhou, W., Chen, C., Buckland, B. and Aunins, J. 1997).
The major drawback of these recombinant Bispecific antibodies is their requirement for efficient dimerization, which is essential for optimal expression and purification. Furthermore, Paul Carter described an “elegant technology which even allowed generation of ‘full-size’ recombinant Bispecific antibodies. Here, heterodimerization of two different heavy chains is enforced by ‘knobs- into-holes’ technology, which ultimately leads to a Bispecific IgG molecule” (Carter, P. 2001). It was observed recently that human antibodies of the IgG4 type can exchange their halves with each other, potentially creating antibodies with dual specificity. Whole antibodies are efficiently produced in mammalian expression systems, where improved culture conditions and expression vectors led to yields of up to 2 g/l for IgG antibodies. In contrast, large-scale production of Bispecific antibodies has proved more difficult.
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