Advances in protein engineering, such as phage display technology, enable us to design antibodies. The recombinant proteins can be expressed in various bacterial hosts, but the expression of antibodies in
E. coli often makes insoluble particles, which is considered to be attributed to the folding process of immunoglobulin-folded structure. In this article, the folding study of immunoglobulin structure is summarized and the refolding procedure for antibody fragments from inclusion bodies is elucidated on the basis of the physicochemical folding study of immunoglobulin structure.
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