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Bobust Binding Proteins of Predetermined Specificity
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We will develop a specific binding protein that has antibody-like diversity but is suitable for higexpression and use in extreme environments. Production of recombinant antibodies in E. coli providessource of active protein for antibody-based technologies, and the small size of the recombinant antisignificant advantages in some applications. However, there are disadvantages attributable to the macomplicated dimeric peptide structure of recombinant antibodies. The bacterial folding and secretionyield high levels of functional expression, especially in the case of Fab. Also, the weakness of assvariable domains often leads to stability problems, especially in case of single- chain Fv. This spean antigen binding site similar to that of antibodies in aspects important for binding and diversitybacterial protein of high thermostability. The design is monomeric, and thus should circumvent foldistability problems associated with recombinant antibody fragments. It should be possible to recoverdesired specificity¿s from a diverse library of these molecules by phage display technology.
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