Bioconjugation: linkage stability and novel methods

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University of Wisconsin--Madison, 2008 - 213 pages
The remarkable stability of amides makes them highly desirable for bioconjugation. We have developed a general method for the site-specific modification of proteins via amide linkages. In this method, proteins are first labeled on their C-termini with the azido functional group by utilizing intein chemistry. Subsequently, a chemoselective amide bond-forming reaction of the azido group---the Staudinger ligation---is performed on the azido-proteins. Using this approach, we have immobilized the ribonuclease A protein rapidly and site-specifically via amide linkages. Furthermore, we have utilized this method to generate azido-single-chain antibodies. Finally, we have improved the scope and the efficiency of this method by integrating it with yeast surface display, to enable the efficient production of both prokaryotic and eukaryotic azido-proteins.

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Contents

Hydrolytic Stability of Hydrazones and Oximes
24
Chapter 3
61
Chapter 4
78
Copyright

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